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
LEVELS OF BIOLOGICAL ORGANIZATION
1. Biosphere
2. Ecosystems Concept 3.3
3. Communities Acidic and basic conditions affect living organisms
4. Populations
The concentration of H+ is expressed as pH
5. Organisms
6. Organs
pH of a solution – the negative logarithm of the hydrogen
7. Tissues
ion concentration
8. Cells
9. Organelles pH 0>7 – increasingly acidic
10. Molecules
pH 7 – neutral pH level; pure water
pH 7>14 – increasingly basic
THE CHEMISTRY OF WATER
Buffer – consists of an acid base pair that combines
reversibly with hydrogen ions, allowing it to resist pH
Concept 3.1
changes
Polar Covalent Bonds in Water result in Hydrogen Bonding
Ocean Acidification – caused by the burning of fossil fuels
Water – polar molecule w/c increases the amount of CO2 in the atmosphere,
- most common molecule in all living things wherein some dissolve in the oceans

CARBON: THE BASIS OF MOLECULAR DIVERSITY

Hydrogen Bond – when partially negatively charged region
on the oxygen of one water molecule is attracted to the
Concept 4.1
partially positively charged hydrogen of a nearby water
Organic Chemistry
molecule

Concept 3.2 Organic Compounds – present in living organisms

Four Emergent Properties of Water - contain carbon
a) Cohesion – Adhesion
• Biological Diversity – results from carbon’s ability to
Cohesion – hydrogen bonding keeps water molecules
form a huge no. of molecules with particular shapes
close to each other
and properties
Adhesion – the clinging of one substance to another
• Living matter – made mostly of Carbon, Oxygen,
Surface Tension – how difficult it is to stretch or break
the surface of a liquid Hydrogen and Nitrogen

Concept 4.2
b) Temperature Regulation
Carbon molecules can form diverse molecules by bonding
Water’s High Specific Heat
to four other atoms
- 1 cal per gram & per degree Celsius
- amount of heat that must be absorbed or lost for 1g
• Carbon – with a valence of 4, can bond to various other
of that substance to change its temperature by 1C
atoms, including O, H, N & Carbon
Thermal Energy – total kinetic energy associated with
the movement of atoms or molecules • Hydrocarbons – consist of carbon & hydrogen
Temperature – average kinetic energy - major components of petroleum (fossil fuel)
Evaporative Cooling – contributes to the stability of
Carbon Skeletons
temperature in the lakes and ponds
- carbon chains form the skeletons of most organic
– based on water’s high heat of vaporization
molecules
- variations:
c) Expansion upon Freezing
a) Length
- water is one of the few substances that is less dense
b) Branching
as a solid than as a liquid; ice floats on liquid water
c) Double bond position
- this property allows life to exist under the frozen
d) Presence of rings
surfaces of lakes and polar seas
Isomers – compounds that have the same molecular
d) Versatility as solvent
- its polar molecules are attracted to ions and polar formula but different structures and properties
substances that can form hydrogen bonds
a) Structural Isomers – differ in covalent arrangements
b) Cis-trans Isomers – carbons have covalent bonds to the
same atoms, but differ in their spatial arrangements
c) Enantiomers – isomers that are mirror images of each
other and differ in shape due to the presence of an
asymmetric carbon
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
c) Hexoses – 6 carbon sugars
a) Linear form – long
b) Ring form – most stable form of sugars
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
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 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

Concept 5.3 Levels of Protein Structure

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
1) Primary – linear chain of amino acids
2) Secondary – regions stabilized by H bonds
between atoms of the polypeptide backbone
3) Tertiary – 3-dimensional shape stabilized by
interactions between side chains
4) Quarternary – association of two or more
polypeptides (some proteins only)

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

Sickle-cell Disease – inherited blood disease
Amino Acid Structure
- 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

20 Amino Acids
• Nonpolar (hydrophobic)
1) Glycine 2) Leucine
4) Alanine 5) Isoleucine
7) Valine 8) Methionine
• Polar (hydrophilic)
10) Serine 11) Cysteine
13) Threonine 14) Tyrosine
• Electrically charged side chains (hydrophilic)
16) Aspartic Acid 17) Lysine
19) Glutamic Acid 20) Arginine
Cysteine – the only amino acid with sulfur
Protein Structure & Function
a) Globular – spherical
b) Fibrous – like long fibers
Concept 5.5
d) Nucleic Acids – polymers made of nucleotides
Gene – controls amino acid sequence of a polypeptide
3) Phenylalanine
6) Tryptophan • DNA (Deoxyribonucleic Acid) – provides direction for
9) Proline its own replication
- genetic material organisms inherit from parents;
stores hereditary info
12) Asparagine - sugar – deoxyribose
15) Glutamine - nitrogenous bases: Adenine (A) – Thymine (T);
Guanine (G) – Cytosine (C)
- double-stranded helix
18) Histidine • 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 Cells
Base sequences = nucleotide sequences - basic structural and functional units of every organism
• Human Genome Project – development of faster & less
expensive methods of sequencing Basic Features of Cells
• Bioinformatics – use of computer software & other a) Plasma Membrane
tools that can handle & analyze large data sets b) Chromosomes
• Genomics – analyzing large sets of genes and c) Ribosomes
comparing whole genomes/different species d) Cytosol – jelly-like substance
• Proteomics – analysis of large sets of proteins,
including sequences Organelles – various functional components found in cells

To Note: Prokaryotic vs. Eukaryotic Cells

Carbon, Hydrogen, Oxygen & Nitrogen a) Prokaryotic Cell (pro-before nucleus)
- make up 96% of atoms • Location of Genetic Material: Nucleoid (no
nucleus)
Structure of Dipeptide Bond • Organelle Characteristics: Lacks an organized
nucleus & other membrane-bound organelles
• Example organisms: Archaea & Eubacteria
(extremophiles)
b) Eukaryotic Cell (eu-true nucleus)

Structure of Saturated vs Unsaturated Fats • Location of Genetic Material: Nucleus

• Organelle Characteristics: Has a true nucleus
surrounded by a complex nuclear membrane
• Example organisms: Amoebae, Plants, Animal,
Fungi & Protists
Structure of Nucleotide
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
- found in the Rough ER, mitochondria, or chloroplasts
• Plasma Membrane – encloses the cytoplasm
- 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
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
a) Flagella b) Cytoplasm c) Ribosomes
d) Cilia e) Cytoskeleton f) Cell Wall
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)
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
• 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 ATP Hydrolysis – supplies the energy for most active
a) Temperature transport
b) Pressure - can induce the protein to change its shape in a manner
c) Space/Charge that translocates a solute bound to the protein across the
d) Hypertonic/Hypotonic – steepness of concentration membrane (ex: sodium-potassium pump)
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 How Ion Pumps maintain Membrane Potential
c) Isotonic – dynamic equilibrium (constant flow) Voltage – electrical potential energy
- no net movement of water across the plasma - separation of opposite charges
membrane
Membrane Potential – voltage across a membrane
Hypertonic Hypotonic Isotonic
Animal Cell Shriveled Swell/Lysed Normal Electrochemical Gradient – combination of chemical and
Plant Cell Plasmolyzed Turgid (Normal) Flaccid 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

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
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... two gradients are accounted for by
contransport proteins
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 • Oxidation - loss of electrons from one substance
- the products of Photosysnthesis and Cellular Respiration • Reduction – addition of electrons to a substance
are the needs of others Reducing agent – electron donor
Oxidizing agent – electron acceptor
Photosynthesis Cellular Respiration
Where Chloroplasts Mitochondria Electron Transport Chain
When In the presence of - consists of molecules, mostly proteins, built into the inner
All the time
light membrane of the mitochondria/eukaryotic cells
Input CO2 & H2O Glucose and O2
Output Glucose and O2 CO2 & H2O Stages of Cellular Respiration
Energy 1) Glycolysis
Light Chemical bonds
Sources - breakdown of glucose (exergonic)
Result Stored Released - begins the degradation process by breaking glucose
into two molecules of a compound called pyruvate,
Mitochondria which enters the mitochondrion (in eukaryotes) and is
• Intermembrane Space – counterpart of stroma oxidized into a compound called acetly CoA, which
• Cristae – folding; counterpart of thylakoid 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

Aerobic – glycolysis to mitochondria

• Glycolysis – inependently aerobic Glucose Production

- yields pyruvate molecules ATP NADH FADH2
- produces lactic acid or ethanol in cytosol if it lacks Glycolysis &
oxygen Pyruvate
2 2 0
• Mitochondria – aerobic Oxidation
- occurs in the presence of O2
- shuttled to mitochondria if O2 is present Citric Acid 0 2 0
Cycle
CELLULAR RESPIRATION
- technically includes both aerobic and anaerobic processes Oxidative 2 6 2
- used to refer to aerobic respiration Phospholyation
- controlled by allosteric enzymes at key points in glycolysis
and citric acid cycle • Malate Apartate Shuttle – 32 ATPs
• Glycerol Phosphate Shuttle – 30 ATPs
Catabolic Pathways
- metabolic pathways that release stored energy by 2) Pyruvate Oxidation & Citric Acid Cycle
breaking down complex molecules - also known as Krebs Cycle
- given the name because Citrate/Citric Acid is the first
Organic compounds – possess potential energy molecule formed
- pyruvate enters the mitochondrion and is oxideized
Fermentation to acteyl CoA
- 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
 Citric Acid Cycle
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
• 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
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 - happens in the stroma surrounding the thylakoid
in temperature affects cholorphyll activation membranes; both at morning and evening as long as
• Chlorophyll – green pigments (A to F) there is ATP & NADPH
• Carotenoids – red to yellow - uses CO2, ATP & NADPH to produce glucose in 6 turns
• Anthocyanines – red, violet & blue - occurs after light reactions
• Phycobilins – red, blue, green, violet & brown Glucose = (6) CO2 G3P = (3) CO2
= (18) ATP = (9) ATP
2 Stages of Photosynthesis = (12) NADPH = (6) NADPH
= (2) G3P

NADPH = (2) photons ATP = (4) H2O

= (1) H2O

LAB NOTES

Parts of a Compound Light Microscope

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
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 Nga pala,
through passive transport Please follow @itssSoGo on Twitter!
• (1) ATP is due to chemiosmosis using 4 Hydrogen ions #ParaSaEntrep