llgure: Collman & uecreau, !"#$% !'$$()% !""#, 3063-3076.

$%&'()*+,- (- /(0,12,-3)(* 4 52,0,&6-02%&(& (- 728,),'8*&0&

CyLochrome c oxldase:
C
2
+ 4P
+
+ 4 e
-
! 2 P
2
C
Peme-Cu oxldase
hoLosysLem ll:
2 P
2
C ! C
2
+ 4P
+
+ 4 e
-
CLC, Mn
4
Ca clusLer
8educuon of molecular C
2
vs. P
2
C oxldauon (waLer-spllmng)
8educuon of molecular C
2
vs. P
2
C oxldauon (waLer-spllmng)
Y244
Cu
B
H240
H376
H290
Fe
II
..Cu
I
: 5. 19
S. Yoshikawa et al. Science, 1998, 280, 1723
H291
Heme a
3
Metal Bridging Mechanism
for O-O Cleavage ??
Heme a
3
- Cu
B
Active-Site
Blomberg, Siegbahn & Wikstrom
Inorg. Chem. 2003, 42, 5231.
Heme-Copper Oxidase Active-Site: O
2
-Reductive Cleavage
Y244
Cu
B
H240
H376
H290
Fe
II
..Cu
I
: 5. 19
S. Yoshikawa et al.
Science, 1998, 280, 1723
H291
Heme a
3
Cu
I
N
N
OH
Fe
III
O
O
Fe
IV
O
Cu
II
OH
N
N
O
P
M
Oxy
Cu
II
N
N
OH
Fe
III
O(H)
O
+ (H
+
)
Cu
B
Heme a
3
H376
Y244
H240
H291
H290
O
2
Cyt. c Oxidase Dioxygen-Reduction: O
2
-Intermediates
G. T. Babcock, Proc. Natl. Acad. Sci. USA 1999, 96, 12971
Fe...Cu = 4.91
FeO = 2.52
CuO = 2.16
OO = 1.63
For discussion of this X-ray structure, see Chem. Rev. 2004, 104, 1077-1133.
Protoctechuate 3,4-Dioxygenase
+H
2
O
+
O
2
- H
2
O
+
O
OH
-
OOC
OH
OH
-
OOC
O
OH
HO Fe
III
O
N
O
His
NH
O
N
NH
HO
Fe
III
His
-
OOC
O
O
O
O
Fe
III
O
HO
-
OOC
O
His
O
N
NH
O
N
NH
O
Fe
III
His
HO
O
O
O
-
OOC
O
O
Fe
II -
OOC
Notes: dioxygenase vs.
monooxygenase; iron
oxidation state does not
change; iron acts as a Lewis
acid; semiradical character of
the catecholate ligand
activates it for direct
attack by the dioxygen
molecule.
!"#$%&'( *+ ,'#-.*/( 0#1#&23'4 52 021*-67*$' 89:;(
CyLochrome 430s caLalyze a <=4' >#7='12 *+ 7'#-.*/(
Some 430s have '"?@=(=1' (@5(17#1' (%'-=A-=12, oLhers exhlblL 57*#4 (@5(17#1' 1*&'7#/-'
Sono, 8oach, CoulLer uawson, !"#$% '#(% BCCD, )*, 2841-2887.
1oday's focus ! hydroxylauon
!"#$
%&'
)&*&+,-% ),%+.

!"#$%"&' !"# %&# '# ()*+,# -.*/0!1# /$$0) 233) *+,-*.+/
resting
state
Note: indicating radical
mechanism here
RH = substrate
!"#$ "& '($ )*"+,-.# /01 2,3.45 .45 6,1'.# /(.*3$ !$#.0

Sono, 8oach, CoulLer uawson, !"#$% '#(% 7889, )*, 2841-2887.
1he proxlmal Cys LhlolaLe provldes 1'*"43 .+,.#
5"4.:"4 '" '($ ;$ <$4'$* (lndlcaLed by wlde
arrow), referred Lo as a blg push," and Lhereby
&.<,#,'.'$1 =>= <#$.?.3$ and 1'.@,#,A$1 ;$BCDE
A 5,1'.# <(.*3$ *$#.0 lnvolvlng 1hr-232 &
Asp-231 ls proposed Lo provlde a proLon
condulL Lo 5$#,?$* F
G
'" ;$HI$*"+" prlor Lo C-
C bond cleavage

Crysta| Structure of Cyanobacter|a| hotosystem II (3.S reso|unon)
lerrelra !"# %&. '()!*(! 2004, +,+, 1831-1838
Sll dlmer sLrucLure ls very lnformauve, buL does noL provlde a denluve sLrucLure of Lhe CLC
Many co-facLors are presenL, chlorophylls are ln green
noLe presence of heme and non-heme lron and locauon of Lhe CLC
Cata|ync Cyc|e of the CLC
llgure: McLvoy & 8rudvlg, -.!/# 0!1# 2006, 2,3, 4433-4483.
S-states ! each oxldauon sLaLe of Lhe CLC ls Lermed a S-sLaLe"
S
o
= leasL oxldlzed, S
4
= mosL oxldlzed
Lach S
n
! S
n+1
trans|non resu|ts |n a 1 e|ectron ox|danon of the CLC meta|-oxo c|uster
1he S
n
! S
n+1
Lransluons requlre llghL (lndlcaLed by llghLenlng bolL)
1he S
4
! S
o
Lransluon ls llghL-lndependenL
oss|b|e Structures of the CLC 8ased on LkAIS
llgure: McLvoy & 8rudvlg, -.!/# 0!1# 2006, 2,3, 4433-4483.
CLC Mode| from the Cyanobacter|a| hotosystem II Crysta|
lerrelra !"# %&. '()!*(! 2004, +,+, 1831-1838
llgure: McLvoy & 8rudvlg, -.!/# 0!1# 2006, 2,3, 4433-4483.
3.3 resoluuon does noL aord a denluve sLrucLure, buL denslLy can be modeled
LlmlLed resoluuon ! -oxo brldges & P-bondlng neLworks are noL resolved
ulscrepancles beLween crysLal sLrucLure and daLa from oLher meLhods
SubsequenLly deLermlned LhaL x-ray damage Lo Lhe Mn
4
Ca complex occurs
Slmplled deplcuon
(noLe dlerenL orlenLauon)
Ass|gnments of CLC L|ectron|c Structure
llgure: ?ano & ?achandra, 4*567# -.!/# 2008, 89, 1711-1726.
AsslgnmenL of CLC elecLronlc sLrucLure ls comp||cated and controvers|a|
L8, l1l8, xAS, uv-vls daLa have conLrlbuLed Lo Lhe currenL model & undersLandlng
1he slgnals below were obLalned uslng Sll lsolaLed from splnach
MLS = mulullne L8 slgnal
CLC Mode| from the Cyanobacter|a| hotosystem II Crysta|
Many mechanlsms for waLer oxldauon by Lhe CLC have been proposed
1wo of Lhese mechanlsms are:
nucleophlllc auack on Mn(v)-C by Ca(ll)-bound waLer or hydroxlde (le)
8eacuon of Lermlnal / brldglng Mn-C unlL wlLh an oxo / hydroxo / waLer llgand (rlghL)
Summary & o|nts to kemember
Mo|ecu|ar oxygen funcuons as a term|na| e|ectron acceptor and b|osynthenc reagent.
naLure uses heme and non-heme lron Lo acuvaLe C
2
and oxldlze subsLraLes.
Cytochrome 4S0s are monooxygenases LhaL can use NAD()n as Lhe elecLron donor. 1hese
enzymes have a Ie(III) resnng state and Lhe Lwo elecLron Lransfers are separaLed by C
2
blndlng.
PeLerolyuc C-C bond cleavage occurs and a Ie(IV)=C porphyr|n p|-rad|ca| canon
Intermed|ate ls LhoughL Lo be Lhe hydroxylaung agenL.
Amlno acld sldechalns of Lhe proLeln tune heme funcuon. 1hls phenomena ls observed for
varlauons ln Lhe ax|a| ||gand of heme-conLalnlng enzymes and for Lhe d|sta| mach|nery.
Cytochrom c ox|dase uullzes heme-le and copper Lo caLalyze Lhe 4-e|ectron reducnon of C
2
Lo
WaLer and provlde a P
+
gradlenL, and ls a case sLudy ln proLon and elecLron Lransfers.
Llke heme enzymes, mononuclear non-heme lron enzymes caLalyze a varleLy of oxldauve
1ransformauons and employ Ie(IV)=C |ntermed|ates. Co-subsLraLes such as !-kC provlde Lhe
necessary reduclng equlvalenLs. 1hese enzymes exhlblL le(ll) resung sLaLes.
hotosystem II ls responslble for water ox|danon and carrles ouL Lhls chemlsLry by uslng a
Mn
4
Ca c|uster.