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Inorganic Chemistry
Outer-sphere Reactions
Inorganic Chemistry
Oxidant with bridging ligands undergoes inner-sphere mechanism. [CoII(CN)5]3- + [CoIII(NH3)5X]2+ [CoIII(CN)5X]3- + [CoII(NH3)5]2+
Substitution 2. ET
Must be outersphere
Outer-sphere Reactions
Tunneling ET
Inorganic Chemistry
1. ET
2. Nuclear reorganization
According to FranckCondon principle Electronic transitions are so fast taking place in a stationary nuclear framework.
Product Reactant
3
Outer-sphere Reactions
Tunneling ET
Inorganic Chemistry
Transition state; Two states are in the same energy! According to Marcus theory The movement of atoms is much slower than that of electrons, so the nuclei Reactant must move before, not during, the electron transfer. Product
Outer-sphere Reactions
ET
Inorganic Chemistry
Td
TBP or SP
Entatic state where Cu(I) geometry is imposed on the Cu (II) site by the protein! Little geometric change on oxidation and a low FranckCondon barrier to ET!
Inorganic Chemistry
1 electron transfer processes are generally preferred. Coupling of proton and electron transfer redox potential control Iron or copper metal ions are typically utilized Electron travels long distances > 10 Structural reorganization Oxidation states Electron transfer rate
1. Iron-Sulfur Proteins
Inorganic Chemistry
Although ultimate proof of the existence of the nFe-nS clusters came from protein XRD data, values for the high-resolution metrical parameters of the clusters and, especially, their overall charge have often relied heavily on the data of the replicative model systems.
Protein Rubredoxin Ferredoxin Ferredoxin Ferredoxin Cluster 1Fe-0S 2Fe-2S 3Fe-4S 4Fe-4S OS Fe3+ Fe2+ Fe3+/3+ Fe2+/3+ Fe3+/3+/3+ Fe2+/3+/3+ Fe2+/3+/3+/3+ Fe2+/2+/3+/3+ Fe2+/2+/2+/3+ EPR
4.3, 9 1.89, 1.95, 2.05 1.97, 2.00, 2.02 2.04, 2.04, 2.12 1.88, 1.92, 2.06
Mssbauer (mm/sec)
0.25 0.65 0.26 0.25, 0.55 0.27 0.30, 0.46 0.31 0.42 0.57
max (nm)
390, 490 310, 335 325, 420, 465 Abs declines 50% 305, 415, 455 425 325, 385, 450 305, 390 Unfeatured 7
Inorganic Chemistry
The protein C. pasteurianum rubredoxin (Rb) A single iron atom Tetrahedral geometry with four sulfur (Cys) atoms; Cys(6)-X-XCys(9)-Gly and Cys(39)-X-X-Cys(42)-Gly HS ferric by EPR and Mssbauer data Oxi form: red color, LMCT band at 490 nm. Redox potentials in the -50 ~ + 50 mV range at pH 7.
Oxi form Fe-S 2.28 Good agreement with synthetic analog bis(oxylyldithiolato)iron(III); Fe-S 2.267 Reduced form Fe-S 2.26~2.32 Good agreement with synthetic analog bis(oxylyldithiolato)iron(II); Fe-S 2.36 The iron center does not change much upon 8 reduction! No CN and Spin state.
Inorganic Chemistry
[2Fe-2S] ferredoxin from S. platensis {Fe2S2(S-Cys)4}2- cluster with two sulfide ligands FeIII-FeIII 2.70 (FeIIFeIII 2.76 EXAFS); <Fe-S-Fe 75 FeIIFeII and FeIIFeIII (mixed-valence form) and FeIIIFeIII Latter two forms exist in the proteins HS in both oxi and reduced forms Antiferromagnetic exchange coupling through two bridging sulfur atoms FeIIFeIII (paramagnetic) and FeIIIFeIII (Diamagnetic) Redox potentials: -280 ~ -490 mV
PDB 1A70
Synthetic model complexes had been prepared and structurally and spectroscopically characterized prior to the protein
Inorganic Chemistry
[3Fe-4S] ferredoxin from A. vinelandii Originally the structure was known as 7-iron ferredoxin; [4Fe-4S] and [3Fe-3S] due to the wrong space group in XRD data. Latter found [3Fe-4S] cluster Fe4S4 cube missing one corner The same cluster was found from Fd from Desulfovibrio gigas and an inactive form of aconitase Redox potentials: -400 mV
Fe-Fe 2.7 , HS FeIIIFeIIIFeIII overall spin 1/2. HS Fe2.5Fe2.5FeIII overall spin 2.
10
Inorganic Chemistry
P. aerogenes Fd [4Fe-4S]2+: FeIIFeIIFeIIIFeIII " 4Fe2.5 fully delocalized Reduced form [4Fe-4S]+: FeIIFeIIFeIIFeIII " fully delocalized as well High-potential iron protein (HiPIP, Chromatium Fd) oxidized form[4Fe-4S]3+: FeIIFeIIIFeIIIFeIII
11
Inorganic Chemistry
The most ubiquitous iron-sulfur clusters in biology A distorted cube Distorted tetrahedral four iron atoms with four sulfide atoms Fe-Fe 2.75 ; S-S 3.55 Model complexes
It can exist in three oxidation states.
P. aerogenes Fd [4Fe-4S]2+: FeIIFeIIFeIIIFeIII " 4Fe2.5 fully delocalized Reduced form [4Fe-4S]+: FeIIFeIIFeIIFeIII " fully delocalized as well High-potential iron protein (HiPIP, Chromatium Fd) oxidized form[4Fe-4S]3+: FeIIFeIIIFeIIIFeIII
2.28
2.31
2.25
Very wide redox potential range: for [4Fe-4S]2+/+ -650 ~ -280 mV for [4Fe-4S]3+/2+ + 350 mV
ET rate constant: 103 104 M-1 s-1 Minimal cluster reorganizational energy
The structural changes at each iron atom are very small. Only 1.3 % changes per added electron!
Inorganic Chemistry
Biological nitrogen reduction by Mo-containing Nitrogenases is the rst identied and well-studied. Fe protein - [4Fe-4S] cluster - MgATP binding site - Dissociated from MoFe Protein after delivering e MoFe protein - 232 K protein with an 22 subunit - P cluster; [8Fe-7S] cluster - FeMo-cofactor: N2 binding
Mackay, B. A., et al. Chem. Rev. 2004, 104, 385; Einsle, O., et al. Science 2002, 297, 1696; Schindelin H., et al. Nature 1997, 387, 370, Rees, D. C. et al. Science 1992, 257, 1653.
Nitrate Reductase
Inorganic Chemistry
Obtained from the sulphate reducing bacterium Desulfavibrio desulfuricans ATCC 27774. A single polypeptide chain of 723 amino acid residues Folded into four domains Molybdenum-containing enzyme bis-molybdopterin guanine dinucleotide (MGD) cofactor One Cys 140 and a water/hydroxo ligand One [4Fe-4S] cluster
Structure 1999, 7, 65
14
Inorganic Chemistry
15
Inorganic Chemistry
EPR
4.3, 9 1.89, 1.95, 2.05 1.97, 2.00, 2.02 2.04, 2.04, 2.12 1.88, 1.92, 2.06
Mssbauer (mm/sec)
0.25 0.65 0.26 0.25, 0.55 0.27 0.30, 0.46 0.31 0.42 0.57
max (nm)
390, 490 310, 335 325, 420, 465 Abs declines 50% 305, 415, 455 425 325, 385, 450 305, 390 Unfeatured 16
Inorganic Chemistry
O-xylyldithiolato ligand
17
Inorganic Chemistry
18
Inorganic Chemistry
Linear Cluster
Cuboidal Cluster
19
Inorganic Chemistry
Cuboidal Cluster
20
Inorganic Chemistry
21
Inorganic Chemistry
22
Inorganic Chemistry
Electron Transfer Protein - Blue mono (Type 1) cupredoxins; plastocyanin (plants), Azurin (bacteria) - Two His, Met, Cys distorted Td - LMCT ~ 600 nm (>3,000 M1cm1) - Very small All value (~ 60 X104 cm1) Very short Cu-S distance ~ 2.1 with very long Met distance. - Eo = + 250 ~ 350 mV, vs. NHE
The site is near the surface of the protein
Entatic state!
SMet
Cu
23
Inorganic Chemistry
Elongated Cu-S
Entatic state! 24
No J-T distortion
Inorganic Chemistry
CuA: Electron Transfer Site - Purple binuclear center; also found in CcO - Two bridging Cys, two His, Met, CarbonlyTrp - 480 nm (~5000 M1cm1), 530 nm (~4000 M1cm1) - Eo = ~ + 240 mV, vs. NHE
SCys Cu Cu SMet SCys O=CTrp
Electron Transfer Protein - Blue mono (T1) cupredoxins; plastocyanin, Azurin - Two His, Met, Cys - ~ 600 nm (5000 M1cm1) - very small All value (~ 60 X104 cm1) - Eo = + 250 ~ 350 mV, vs. NHE
SMet
Cu
SCys
e
Trp N O Cu N N
CuI CuI
Cu1.5 Cu1.5
e
Plastocyanin PDB code: 1PLC
N Cu S
S
2.47
- - - -
25
Inorganic Chemistry
Homotrimer with 36 kDa monomer Three identical subunits are tightly associated around a 3-fold axis to form a trimer around a central channel of 5-6 . Each monomer contains type 1 copper (2 His, 1 Met and 1 Cys) and type 2 copper (3 His and solvent) Intense 593 nm absorption band (3,800 M-1 cm-1) due to LMCT in type 1 copper. can be classified into two group green or blue.
12.6
Acc. Chem. Res. 2000, 33, 728-735
26
Inorganic Chemistry
PHM (Peptidylglycine -Hydroxylating Monooxygenase) catalyzes stereo-specific hydroxylation of a glycine -carbon in peptide amidation of many neuropeptides and peptide hormones.
H N
H N O
O H OH N COOH R H
H atom abstraction
O
H N
O H N COOH R H
Prigge S. T. et al., Science 1997, 278, 1300-1305; 27 Prigg e S. T. et al., Cell. Mol. Life Sci. 2000, 57, 1236-1259
Inorganic Chemistry
Head-to-tail homodimer
SCys Cu Cu SMet SCys O=CTrp
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Inorganic Chemistry
-diketiminate
Utilizing the same Triphenylmethylthiolate ligand Axial ligand exists in complex 1 but not in complex 2.
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3. Cytochromes
Inorganic Chemistry
The final class of ET proteins utilizing iron porphyrins Most cytochromes have two axial ligands, affording coordinately saturated octahedral complexes. Eukaryotic cytochrome c uses His and Met. In addition, the prosthetic group is bound to covalently via two thioether linkages. Two propionic acid substituents is exposed to solvent.
LS Fe(II/III)
Why?
Nonbonding T2g
Propionic acid
30
Inorganic Chemistry
31
Inorganic Chemistry
TM domain: 13 helices span the transmembrane region Two heme b and b3 and one none-heme iron, FeB Globular hydrophilic domain: heme c. NOR is an evolutionary progenitor of cytochrome oxidases.
The topology of the TM region and the arrangement of the metal centers in cNOR are similar to those of cytochrome oxidases, a superfamily of enzymes that act as the terminal oxidases in aerobic respiratory transport chains.
32
Inorganic Chemistry
M207 C200
CuA
CuA
C196 E198
H204
H291
CuB
H376 H378
H290 H24 0
Heme a3 Heme a!