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LEVELS OF BIOLOGICAL ORGANIZATION 1. Biosphere 2. Ecosystems 3. Communities 4. Populations 5. Organisms 6.
LEVELS OF BIOLOGICAL ORGANIZATION 1. Biosphere 2. Ecosystems 3. Communities 4. Populations 5. Organisms 6.
LEVELS OF BIOLOGICAL ORGANIZATION 1. Biosphere 2. Ecosystems 3. Communities 4. Populations 5. Organisms 6.

LEVELS OF BIOLOGICAL ORGANIZATION

1. Biosphere

2. Ecosystems

3. Communities

4. Populations

5. Organisms

6. Organs

7. Tissues

8. Cells

9. Organelles

10. Molecules

THE CHEMISTRY OF WATER

Concept 3.1 Polar Covalent Bonds in Water result in Hydrogen Bonding

Water – polar molecule - most common molecule in all living things

Hydrogen Bond when partially negatively charged region on the oxygen of one water molecule is attracted to the partially positively charged hydrogen of a nearby water molecule

Concept 3.2

Four Emergent Properties of Water

a) Cohesion – Adhesion Cohesion – hydrogen bonding keeps water molecules close to each other Adhesion – the clinging of one substance to another Surface Tension – how difficult it is to stretch or break the surface of a liquid

b) Temperature Regulation Water’s High Specific Heat

- 1 cal per gram & per degree Celsius

- amount of heat that must be absorbed or lost for 1g

of that substance to change its temperature by 1C Thermal Energy – total kinetic energy associated with the movement of atoms or molecules Temperature – average kinetic energy Evaporative Cooling – contributes to the stability of temperature in the lakes and ponds – based on water’s high heat of vaporization

c) Expansion upon Freezing

- water is one of the few substances that is less dense

as a solid than as a liquid; ice floats on liquid water

- this property allows life to exist under the frozen surfaces of lakes and polar seas

d) Versatility as solvent

- its polar molecules are attracted to ions and polar substances that can form hydrogen bonds

Solution – homogenous mixture of 2/more substances Solvent – dissolving agent of a solution Solute – substance that is dissolved Hydrophilic – substances that are attracted to water Hydrophobic – substances not attracted to water Molarity – number of moles of solute per L of solution

Concept 3.3 Acidic and basic conditions affect living organisms

The concentration of H+ is expressed as pH

pH of a solution – the negative logarithm of the hydrogen ion concentration pH 0>7 – increasingly acidic pH 7 – neutral pH level; pure water pH 7>14 – increasingly basic

Buffer – consists of an acid base pair that combines reversibly with hydrogen ions, allowing it to resist pH changes Ocean Acidification – caused by the burning of fossil fuels w/c increases the amount of CO2 in the atmosphere, wherein some dissolve in the oceans

CARBON: THE BASIS OF MOLECULAR DIVERSITY

Concept 4.1

Organic Chemistry

Organic Compounds – present in living organisms

- contain carbon

Biological Diversity – results from carbon’s ability to form a huge no. of molecules with particular shapes and properties

Living matter – made mostly of Carbon, Oxygen, Hydrogen and Nitrogen

Concept 4.2 Carbon molecules can form diverse molecules by bonding to four other atoms

Carbon – with a valence of 4, can bond to various other atoms, including O, H, N & Carbon

Hydrocarbons – consist of carbon & hydrogen - major components of petroleum (fossil fuel)

Carbon Skeletons

- carbon chains form the skeletons of most organic molecules

- variations:

a) Length

b) Branching

c) Double bond position

d) Presence of rings

Isomers – compounds that have the same molecular formula but different structures and properties

a) Structural Isomers – differ in covalent arrangements

a) Structural Isomers – differ in covalent arrangements b) Cis-trans Isomers – carbons have covalent bonds

b) Cis-trans Isomers – carbons have covalent bonds to the same atoms, but differ in their spatial arrangements

to the same atoms, but differ in their spatial arrangements c) Enantiomers – isomers that are

c) Enantiomers – isomers that are mirror images of each other and differ in shape due to the presence of an asymmetric carbon

differ in shape due to the presence of an asymmetric carbon Concept 4.3 ATP (Adenosine Triphosphate)

Concept 4.3 ATP (Adenosine Triphosphate)

- consists of adenosine attached to three phosphate groups

- reacts with water, forming ADP (Adenosine Diphosphate)

and inorganic phosphate, which releases energy that can be used by the cell

BIOLOGICAL MACROMOLECULES AND LIPIDS

Concept 5.1 Macromolecules are polymers, built from monomers

Polymers – large carbohydrates (polysaccharides), proteins and nucleic acids

- chains of monomers

Monomers – repeating units that serve as the building

blocks of a polymer

Enzymes – macromolecules that speed up chemical reactions

Dehydration Reaction – reaction in which two molecules are covalently bonded to each other with the loss of a water molecule

Hydrolysis – disassembly of monomers

- reverse of dehydration reaction

- water (Greek: Hydro) breakage (lysis)

Large Biological Molecules

Concept 5.2

a) Carbohydrates – includes sugar & polymers Monosaccharides – single (monos); sugar (sacchar)

- molecular formulas are the multiple of CH2O

Glucose (C6H12O6) – most common monasaccharide

Structure of Monasaccharides

Aldoses – carbonyl group at end of carbon skeleton Ketoses – carbonyl group within carbon skeleton

a) Trioses – 3 carbon sugars

b) Pentoses – 5 carbon sugars

a) Linear form – long

b) Pentoses – 5 carbon sugars a) Linear form – long b) Ring form – most

b) Ring form – most stable form of sugars

form – long b) Ring form – most stable form of sugars Disaccharides – 2 monosaccharides

Disaccharides – 2 monosaccharides joined by a glycosidic linkage

- formed through dehydration reaction

Maltose – glucose + glucose Sucrose – glucose + fructose Lactose – present in milk

Polysaccharides – hundred-thousand monosaccharides

a) Storage Polysaccharides - stores sources of energy

- present in starch (plants), glycogen (liver of

animals)

b) Structural Polysaccharides - structure

- cellulose (plants), chitin (exoskeleton of insects)

Microfibrils – parallel cellulose molecules held together

Concept 5.3

b) Lipids – large biological molecules that do not include

true molecules

- mix poorly with water

1)

Fats – not polymers; blended by dehydration reaction Glycerol -backbone of fat/triglyceride Fatty Acid – long carbon skeleton; hydrophobic

Fatty Acid – long carbon skeleton; hydrophobic Saturated Fats – with many hydrogen atoms - solid

Saturated Fats – with many hydrogen atoms

-

solid in room temperature (lard, butter, most

animal fats) Unsaturated Fats – has one/more double bonds; less Hydrogen

-

liquid in room temperature (olive, cod liver oil)

Trans Fats – contribute to coronary heart disease

2)

Phospholipids – has a hydrophilic (polar) head, 2 hydrophobic (nonpolar) tails

3)

Steroids – characterized by a carbon skeleton w/ 4 fused rings

- where sex hormones are synthesized

Ester Linkages

Ester Linkages Concept 5.3 c) Proteins – accounts for 50% of the dry mass of cells

Concept 5.3

c) Proteins – accounts for 50% of the dry mass of cells

- regularize metabolism by acting as catalysts

Catalysts - workhorses

- chemical agents that selectively speed up chemical reactions without being consumed in the reaction

Peptide Bond – bond between amino acids Polypeptide Bond – polymer of amino acids

Amino Acids (Monomers) – organic molecules with both an amino group and carbonyl group R group/Side Chain – differs w/ each amino acid

1)

Enzymatic Proteins – catalyze chemical reactions

2)

Defensive Proteins – protect against disease

3)

Storage Proteins – store amino acids

4)

Transport Proteins – transport substances

5)

Hormonal – coordinate organismal responses

6)

Receptor – receive signals from outside cells

7)

Motor Proteins – function in cell movement

8)

Structural Proteins – provide structural support

Disulfide Bridge – causes the folding of proteins

Amino Acid Structure

– causes the folding of proteins Amino Acid Structure 20 Amino Acids • Nonpolar (hydrophobic) 1)

20 Amino Acids

Nonpolar (hydrophobic)

1)

Glycine

2)

Leucine

3)

Phenylalanine

4)

Alanine

5)

Isoleucine

6)

Tryptophan

7)

Valine

8)

Methionine

9)

Proline

Polar (hydrophilic)

 

10) Serine

 

11) Cysteine

12) Asparagine

13) Threonine

14) Tyrosine

15) Glutamine

Electrically charged side chains (hydrophilic)

16) Aspartic Acid

19) Glutamic Acid 20) Arginine

17) Lysine

18) Histidine

Cysteine – the only amino acid with sulfur

Protein Structure & Function

a) Globular – spherical

b) Fibrous – like long fibers

Models

a) Space-filling – shows all of the atoms

b) Ribbon – only shows backbone of polypeptide

c) Wireframe – shows backbone of polypeptide chain w/ side chains

X-ray Crystallography – used to generate a computer model of an antibody protein

Levels of Protein Structure

1)

Primary – linear chain of amino acids

2)

Secondary – regions stabilized by H bonds

3)

between atoms of the polypeptide backbone Tertiary – 3-dimensional shape stabilized by interactions between side chains

4)

Quarternary – association of two or more polypeptides (some proteins only)

association of two or more polypeptides (some proteins only) Sickle-cell Disease – inherited blood disease -

Sickle-cell Disease – inherited blood disease

- caused by substitution of one amino acid (Valine) for the normal one (glutamic acid)

- angular cells clog tiny blood cells

Denaturation – unraveling of protein, losing its shape

Concept 5.5

d) Nucleic Acids – polymers made of nucleotides Gene – controls amino acid sequence of a polypeptide

DNA (Deoxyribonucleic Acid) – provides direction for its own replication

- genetic material organisms inherit from parents; stores hereditary info

- sugar – deoxyribose

- nitrogenous bases: Adenine (A) – Thymine (T); Guanine (G) – Cytosine (C)

- double-stranded helix

RNA (Ribonucleic Acid) – directed by DNA to control protein synthesis

- various functions in gene expression

- sugar – ribose

- nitrogenous bases: Adenine (A) – Uracil (U); Guanine (G) – Cytosine (C)

- single-stranded helix

Concept 5.6 Base sequences = nucleotide sequences • Human Genome Project – development of faster

Concept 5.6 Base sequences = nucleotide sequences

Human Genome Project – development of faster & less expensive methods of sequencing

Bioinformatics – use of computer software & other tools that can handle & analyze large data sets

Genomics – analyzing large sets of genes and comparing whole genomes/different species

Proteomics – analysis of large sets of proteins, including sequences

To Note:

Carbon, Hydrogen, Oxygen & Nitrogen - make up 96% of atoms

Structure of Dipeptide Bond

- make up 96% of atoms Structure of Dipeptide Bond Structure of Saturated vs Unsaturated Fats

Structure of Saturated vs Unsaturated Fats

Dipeptide Bond Structure of Saturated vs Unsaturated Fats Structure of Nucleotide Cells - basic structural and

Structure of Nucleotide

of Saturated vs Unsaturated Fats Structure of Nucleotide Cells - basic structural and functional units of
of Saturated vs Unsaturated Fats Structure of Nucleotide Cells - basic structural and functional units of

Cells - basic structural and functional units of every organism

Basic Features of Cells

a) Plasma Membrane

b) Chromosomes

c) Ribosomes

d) Cytosol – jelly-like substance

Organelles various functional components found in cells

Prokaryotic vs. Eukaryotic Cells

a) Prokaryotic Cell (pro-before nucleus)

Location of Genetic Material: Nucleoid (no nucleus)

Organelle Characteristics: Lacks an organized nucleus & other membrane-bound organelles

Example organisms: Archaea & Eubacteria (extremophiles)

b) Eukaryotic Cell (eu-true nucleus)

Location of Genetic Material: Nucleus

Organelle Characteristics: Has a true nucleus surrounded by a complex nuclear membrane

Example organisms: Amoebae, Plants, Animal, Fungi & Protists

Animal Cell vs. Plant Cell
Animal Cell vs. Plant Cell

Terms to Remember:

Fimbriae – attachment structures on the surface of some prokaryotes

Nucleoid – region where DNA is located

Ribosomes – complexes that synthesize proteins

Cytosol vs. Cytoplasm

- Cytosol is a jelly-like fluid substance found in all cells, while the Cytoplasm is the interior of both types of cells (except nucleus)

Cell components that are not membrane bound

-

found in the Rough ER, mitochondria, or chloroplasts

a)

Flagella

b)

Cytoplasm

c)

Ribosomes

Plasma Membrane – encloses the cytoplasm

d)

Cilia

e)

Cytoskeleton

f)

Cell Wall

- selective barrier that allows passage of enough

oxygen, nutrients and waste products

Cell Wall – rigid structure outside the cytoplasm

Glycocalyx – outer coating of many prokaryotes

Cytoplasm – region betwwn the nucleus and the plasma membrane (in eukaryotic cells)

Cytoskeleton – reinforces cell’s shape; functions in cell movement

Microvilli – projections that increase the cell’s surface area

Peroxisome – specialized metabolic compartment bounded by a single membrane

- produces hydrogen peroxide as a by-product and then

converts it to water

Chromatin – material consisting of DNA and proteins

Plasmodesmata – cytoplasmic channels through cell walls that connect the cytoplasms of adjacent cells

Nuclear Envelope – encloses the nucleus

Nuclear Lamina – net-like array of protein filaments

Vesicles – sacs made of membrane

Endoplasmic Reticulum (ER) – extensive network of membranes that accounts for more than half of the total membranes in eukaryotic cells

Glycoproteins – proteins with carbohydrates covalently bonded to them

Phagocytosis – amoeba & other unicellular eukaryotes engulfing smaller organisms/food particles

Thylakoid – membranous system in the form of flattened, interconnected sacs

Granum – each stack of thylakoids (plural: grana)

Stroma – fluid outside thylakoids

Centrosome – area outside of the nucleus

Centrioles – composed of nine sets of triplet microtubules arranged in a ring

Cortex – outer cytoplasmic layer of a cell

Compartamentalization – formation of cellular

compartments in the form of membrane-bound structures

- helps in separating biochemical reactions

Autophagy – process of cellular digestion

- allows the orderly degradation and recycling of cellular components

Cell destruction by self-digestion depends on the amount of enzymes leaked by a lysosome

The inner membrane of the mitochondria has convolutions and infoldings to provide more surface area for cellulare respiration

Organelles responsible for the movement in and of the cell

a) Cytoplasm

b) Cilia

c) Flagella

Mitochondria and Chloroplast are not included in the endomembrane system because they function differently from the organelles that regulate protein traffic and metabolic processes. They transform energy they acquire from their surroundings

Endosymbiont Theory – states that an early ancestor of eukaryotic cells engulfed an oxygen-using nonphotosynthetic prokaryotic cell. Eventually, the engulfed cell formed a relationship with the host cell in which it was enclosed, becoming an endosymbiont (cell living within another cell)

CELL MEMBRANES

Concept 8.1 Plasma Membrane/Cell Membrane

- boundary that separates a living cell from its surroundings

- controls all inbound and outbound traffic

- made up of a phospholipid bilayer

- held together by hydrophobic interactions

- fluid mosaic (collage of different proteins – at least 50)

fluid mosaic (collage of different proteins – at least 50) Lipids and proteins – staple ingredients

Lipids and proteins – staple ingredients of membranes

Phospholipids – most abundant lipids in most membranes

- amphiphatic (hydrophilic head and hydrophobic tail)

Cholesterol wedged between phospholipid molecules in the plasma membrane of animal cells

- has different effects on membrane fluidity at different temperatures; fluidity buffer of the membrane

- reduces membrane fluidity at moderate temperatures

which affects its permeability and ability to function

- travels in the blood in particles called low-density lipoproteins (LDLs)

Membrane Proteins

Integral Proteins – penetrate the hydrophobic interior of the lipid bilayer

- majority are transmembrane proteins which span the membrane

Peripheral Proteins – not embedded in the lipid bilayer at all; held in place by attachment to the cytoskeleton

Some Functions of Membrane Proteins

a) Transport – serves as a hydroliphic channel across the membrane

b) Enzymatic Activity – carries out sequential steps of a metabolic pathway

c) Signal transduction – a membrane protein may have a binding site with a specific shape that fits the shape of a chemical messenger

d) Cell-cell recognition – some glycoproteins serve as ‘identification tags’ that are recognized by membrane proteins of other cells

- cell’s ability to distinguish one type of neighboring cell from another

e) Intercellular jointing – membrane proteins may hook together in various kinds of junctions (gap/tight)

f) Attachment to the cytoskeleton and extracellular matrix (ECM) – proteins that can bind to ECM molecules can coordinate extracellular and intracellular changes

can coordinate extracellular and intracellular changes • Glycolipids – membrane carbohydrates covalently

Glycolipids – membrane carbohydrates covalently bonded to lipids

Glycoproteins – membrane carbohydrates covalently bonded to proteins

Concept 8.2 Membrane Structure results in Selective Permeability

Biological Membrane – example of a supramolecular structure

Transport Proteins where hydrophilic substances pass through to avoid contact with the lipid bilayer

Channel Proteins – function by having a hydrophilic channel that certain molecules/atomic ions use as a tunnel through the membrane

Aquaporins – channel proteins through which water molecules pass through the plasma membrane

- helical regions of a membrane transport channel protein

Carrier Proteins – hold onto their passengers and change shape in a way that shuttles them across the membrane

Selective Permeability – allows certain substances to cross more easily than others

In – hydrophobic/non-polar molecules

- steroids, fats and oils

a) Gases (O2, CO2, N2)

b) Small uncharged polar molecules (H2O, ethanol, urea)

Out – hydrophilic/polar molecules

- glucose

a) Ions (Na+, H+, HOO3-)

b) Charged Molecules (proteins, nucleic acids, amino acids)

Concept 8.3 Passive Transport – diffusion of a substance across a biological membrane wherein the cell does not have to expend energy to make it happen

Diffusion – movement of particles “along” the concentration gradient so that they spread out into the available space

- transport of molecules w/ high concentration towards a membrane

- spontaneoud process needing no input of energy

Concentration Gradient – region along which the density of a chemical substance increases or decreases

- difference in solute concentration between adjacent regions of solution

Osmosis – diffusion of free water across a selectively permeable membrane

5 Factors Affecting the Rate of Diffusion

a) Temperature

b) Pressure

c) Space/Charge

d) Hypertonic/Hypotonic – steepness of concentration gradient

e) Size of atomic molecules

Tonicity – ability of a surrounding solution to cause a cell to gain or lose water

a) Hypertonic – more solute; less H2O

- cell will lose water, shrivel, and probably die

b) Hypotonic – less solute; more H2O

- water will enter the cell faster than it leaves

c) Isotonic – dynamic equilibrium (constant flow)

- no net movement of water across the plasma membrane

 

Hypertonic Hypotonic

Isotonic

Animal Cell

Shriveled

Swell/Lysed

Normal

Plant Cell

Plasmolyzed Turgid (Normal) Flaccid

Normal Plant Cell Plasmolyzed Turgid (Normal) Flaccid Osmoregulation – control of solute concentration and

Osmoregulation – control of solute concentration and water balance

Turgor Pressure – expansion of inelastic cell wall only so much before it exerts a back pressure on the cell

Turgid (very firm) – healthy state for most plant cells

Flaccid (limp) – the plant wilts

Plasmolysis – occurs when plasma membranes pull away from the cell at multiple places

- causes plants to wilt and die

Facilitated Diffusion – passive diffusion of polar molecules and ions impeded by the lipid bilayer of the membrane with the help of transport proteins

a) Ion Channels – channel proteins that transport ions

b) Gated Channels – open/close in response to a stimulus

Concept 8.4 Active Transport – uses energy to move solutes against their gradients

- enables a cell to maintain internal concentartions of small solutes

ATP Hydrolysis – supplies the energy for most active transport

- can induce the protein to change its shape in a manner

that translocates a solute bound to the protein across the

membrane (ex: sodium-potassium pump)

the protein across the membrane (ex: sodium-potassium pump) How Ion Pumps maintain Membrane Potential Voltage –

How Ion Pumps maintain Membrane Potential Voltage – electrical potential energy

- separation of opposite charges

Membrane Potential voltage across a membrane

Electrochemical Gradient – combination of chemical and electrical forces acting on diffusion of ions

Electrogenic Pump – transport protein that generates voltage across a membrane

Proton Pump – electrogenic pumps that store energy by generating voltage across membranes

Cotransport – transport protein that can couple the “downhill” diffusion of the solute to the “uphill” transport of a second substance against its own concentration gradient

Coupled Transport

- occurs when active transport of a solute indirectly drives the transport of another solute

- indirectly uses ATP from active transport

- two proton pumps

contransport proteins

two gradients are accounted for by

Concept 8.5 Bulk Transport – across the plasma membrane by exocytosis and endocytosis

- crossing of proteins and polysaccharides packaged in vesicles

- also require energy like active transport

Exocytosis – cell secretion of certain molecules by the fusion of vesicles with the plasma membrane

- used by many secretory cells to export products

Endocytosis – the cell takes in molecules and particulate matter by forming new vesicles from the plasma membrane

- looks like the reverse of exocytosis

a) Phagocytosis (cellular eating)

- cell engulfs a particle by extending pseudopodia

b) Pinocytosis (cellular drinking)

- cell continuously ‘gulps’ droplets of extracellular

fluid into tiny vesicles

c) Receptor-mediated Endocytosis

- specialized type of pinocytosis that enables the cell to acquire bulk quantities of specific substances

BIOENERGETICS

- the products of Photosysnthesis and Cellular Respiration are the needs of others

Where

When

Input

Output

Energy

Sources

Result

Photosynthesis Chloroplasts In the presence of light CO2 & H2O Glucose and O2

Light

Stored

Cellular Respiration Mitochondria

All the time

Glucose and O2 CO2 & H2O

Chemical bonds

Released

Mitochondria

Intermembrane Space – counterpart of stroma

Cristae – folding; counterpart of thylakoid

stroma • Cristae – folding; counterpart of thylakoid Aerobic – glycolysis to mitochondria • Glycolysis –

Aerobic – glycolysis to mitochondria

Glycolysis – inependently aerobic

- yields pyruvate molecules

- produces lactic acid or ethanol in cytosol if it lacks oxygen

Mitochondria – aerobic

- occurs in the presence of O2

- shuttled to mitochondria if O2 is present

CELLULAR RESPIRATION

- technically includes both aerobic and anaerobic processes

- used to refer to aerobic respiration

- controlled by allosteric enzymes at key points in glycolysis and citric acid cycle

Catabolic Pathways

- metabolic pathways that release stored energy by breaking down complex molecules

Organic compounds – possess potential energy

Fermentation

- partial degradation of sugars/other organic fuel that occurs without the use of oxygen

Aerobic Respiration

- oxygen is consumed as a reactant

Redox Reaction

- also known as oxidation-reduction reactions

- transfer of electrons from one reactant to another

Oxidation - loss of electrons from one substance

Reduction – addition of electrons to a substance Reducing agent – electron donor Oxidizing agent – electron acceptor

Electron Transport Chain - consists of molecules, mostly proteins, built into the inner membrane of the mitochondria/eukaryotic cells

Stages of Cellular Respiration

1)

Glycolysis

 

- breakdown of glucose (exergonic)

 

- begins the degradation process by breaking glucose

into two molecules of a compound called pyruvate, which enters the mitochondrion (in eukaryotes) and is

oxidized into a compound called acetly CoA, which enters the Citric Acid Cycle

-

in prokaryotes, this process occurs in the cytosol

uses glucose and produces 2 Pyruvate, 2 ATP and 2NADH per glucose molecule

-

 
 

Glucose Production

 
 

ATP

NADH

FADH2

 

Glycolysis &

Pyruvate

Oxidation

2

2

0

Citric Acid

0

2

0

Cycle

Oxidative

2

6

2

Phospholyation

 

Malate Apartate Shuttle – 32 ATPs

 

Glycerol Phosphate Shuttle – 30 ATPs

2)

Pyruvate Oxidation & Citric Acid Cycle

 

- also known as Krebs Cycle

- given the name because Citrate/Citric Acid is the first molecule formed

- pyruvate enters the mitochondrion and is oxideized to acteyl CoA

Citrate/Citric Acid is the first molecule formed - pyruvate enters the mitochondrion and is oxideized to

Citric Acid Cycle

Citric Acid Cycle 3) Oxidative Phosphorylation - electron transport and chemiosmosis - powered by the redox

3)

Oxidative Phosphorylation

- electron transport and chemiosmosis

- powered by the redox reactions of the electron

transport chain

- more ATP produced inside mitochondria

- accounts for 90% of the ATP generated by respiration

- like photosynthesis

- NADH & FADH2 transfer electrons to the electron transport chain

- electrons move down the chain, losing energy in

several energy-releasing steps

- electron transfer causes the protein complexes to move H from the mitochondrial matrix to the

intermembrane space, storing energy as proton- motive force

Chemiosmosis – takes place in the plasma membrane

- phosphorylation of ADP to form ADP

Anaerobic Respiration

- an electron transport chain is present with a final electron acceptor rather than oxygen

Fermentation

- electrons from NADH are passed to pyruvate or a

derivative of pyruvate, regenerating the NAD required to

oxidize more glucose

- ex: alcohol fermentation, lactic acid fermentation

Oxygen – good antioxidant

- last receptor

Water – last receiver of electron

Neuronal Synapses – use of ATP to perform Factors : Stress, Hunger, Lack of sleep, & dehydration

Increase of stress hormones decreases respiration; activates production of cortisol

PHOTOSYNTHESIS

- occurs in plants, algae, certain unicellular eukaryotes, some prokaryotes

- source of earth’s oxygen

Leaves – major site of photosynthesis in plants

Autotrophs – self-feeders; producers of the biosphere

- sustain themselves without eating anything derived from other living beings

- produce own organic molecules from CO2 and other

inorganic raw materials

- ex: multicellular alga (kelp), unicellular protists (Euglena sp.), Cyanobacteria

Photoautotrophs – organisms that use light as a source of energy to synthesize organic substances

Chemoautotrophs – use chemicals in their external environment to synthesize (chemosynthesis)

- ex: Purple sulfur bacteria

Heterotrophs – consumers; unable to make own food

- obtain organic material by eating/consuming autotrophs

- ex: human, animals, fungi

Chloropalsts – celllular organelles present in plants and other photosynthetic organisms

- found mainly in cells of the mesophyll

organisms - found mainly in cells of the mesophyll • Stomata – microscopic pores where CO2

Stomata – microscopic pores where CO2 enters

Stroma – dense fluid inside the chloroplast

Thylakoids – segregates the stroma from the thylakoid space inside the sacs

- made up of phospholipid bilayers

- stacked in columns called grana (singular: granum)

Chlorophyll – green pigment of leaves

Process

1. Chloroplasts capture light energy

2. Water enters the leaf

3. Carbon dioxide enters the leaf through the stomata

4. Using the captured light energy, glucose and oxygen are produced inside the chloroplasts through a complete series of chemical reactions

chloroplasts through a complete series of chemical reactions Used: H – 12; O – 18; C

Used: H – 12; O – 18; C – 6

ATP Synthase

- an enzyme that makes ATP and a carrier protein; helps H ions cross the thylakoid membrane

Accessory Pigments

2.

Light-independent reaction / Calvin Cycle

- commonly activated during autumn, where drastic change in temperature affects cholorphyll activation

Chlorophyll – green pigments (A to F)

Carotenoids – red to yellow

Anthocyanines – red, violet & blue

Phycobilins – red, blue, green, violet & brown

2 Stages of Photosynthesis

blue, green, violet & brown 2 Stages of Photosynthesis 1. Light-dependent reaction - uses water, light

1. Light-dependent reaction

- uses water, light energy, and chlorophyll to produce

oxygen molecules, as well as ATP & NADPH

- process wherein light energy is converted to chemical

energy

Photosystems – light catchers

- absorb and refelect rainbow colors

- Photosystem II comes before Photosystem I because PI was discovered first

a) Photosystem II – absorbs photons; chlorophyll becomes ‘excited’; results to the loss of one electron

b) Photosystem I – electron transfer; replacing lost electron through light reaction; travels up to electron receptors (NADP + H) and turns into NADPH which is used in the light-independent reaction

Electron Transport Chain

- production of NADPH, use of 2 photons of light

- occurs in the thylakoid membranes

Chemiosmotic gradient

- causes H ions to flow across the thylakoid to the stroma

- causes H ions to flow across the thylakoid to the stroma - happens in the

- happens in the stroma surrounding the thylakoid

membranes; both at morning and evening as long as there is ATP & NADPH

- uses CO2, ATP & NADPH to produce glucose in 6 turns

- occurs after light reactions

Glucose

= (6) CO2

G3P

= (3) CO2

= (18) ATP

= (9) ATP

= (12) NADPH

= (6) NADPH

= (2) G3P

NADPH

= (2) photons

ATP

= (4) H2O

LAB NOTES

= (1) H2O

Parts of a Compound Light Microscope

H2O LAB NOTES = (1) H2O Parts of a Compound Light Microscope Field of View/Vision –

Field of View/Vision – area that can be seen under the ocular/eyepiece Depth of Field – thickness of the object in sharp focus

Ocular Micrometer – small glass disk with etched lines and numbers arranged in a row Stage Micrometer – with lines of a standard ruler

Magnifications/Objectives

Ocular – 10x

Scanner (Red) – 4x (10X) = 40x

Low Power Objective (LPO; Yellow) – 10x (10x) = 100x

High Power Objective (HPO; Blue) – 40x (10x) = 400x

Oil Immersion (OIO; White) – 100x (10x) = 1000x

Cedar Oil – used for observing very small viruses and bacteria

Make and break (Photolysis) of water (x2)

#LahatKaya

-

H+, H+, O-, H+, H+, O-

#ParaSaDiploma

O2 will be produced outide, but Hydrogen ions will remain inside with high concentration; goes out through passive transport

(1) ATP is due to chemiosmosis using 4 Hydrogen ions

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