 |
PDBsum entry 1frm
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
1frm
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Biol Chem
269:8564-8575
(1994)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4FE-4S]2+/+ cluster reduction potential.
|
|
B.Shen,
D.R.Jollie,
C.D.Stout,
T.C.Diller,
F.A.Armstrong,
C.M.Gorst,
G.N.La Mar,
P.J.Stephens,
B.K.Burgess.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The structures of Azotobacter vinelandii ferredoxin I (AvFdI) and Peptococcus
aerogenes ferredoxin (PaFd), near their analogous [4e-4S]2+/+ clusters, are
highly conserved (Backes, G., Mino, Y., Loehr, T.M., Meyer, T.E., Cusanovich,
M.A., Sweeney, W.V., Adman, E.T., and Sanders-Loehr, J. (1991) J. Am. Chem. Soc.
11, 2055-2064). Despite these similarities, the reduction potential (E0') of the
AvFdI [4Fe-4S]2+/+ cluster is more than 200 mV more negative than that of PaFd.
We have tested the contribution that individual amino acid residues make to the
control of E0' by converting residues in AvFdI into the corresponding residue in
PaFd. Four mutations involved substitutions of negatively charged surface
residues with neutral residues and two involved substitution of buried
hydrophobic residues. All AvFdI variants were characterized by x-ray
crystallography, absorption, CD, EPR, and 1H NMR spectroscopies and by
electrochemical methods. For the F25I mutation, significant structural changes
occurred that affected the EPR and 1H NMR spectroscopic properties of AvFdI and
had a minor influence on E0'. For all other mutations there were no changes in
reduction potential. Thus we conclude, that variations in charged surface
residues do not account for the observed differences in E0' between the
analogous [4Fe-4S]2+/+ cluster of PaFd and AvFdI. These differences are
therefore most likely to be due to differences in solvent accessibility.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
Y.Luo,
C.E.Ergenekan,
J.T.Fischer,
M.L.Tan,
and
T.Ichiye
(2010).
The molecular determinants of the increased reduction potential of the rubredoxin domain of rubrerythrin relative to rubredoxin.
|
| |
Biophys J,
98,
560-568.
|
|
|
|
|
|
|
P.Giastas,
N.Pinotsis,
G.Efthymiou,
M.Wilmanns,
P.Kyritsis,
J.M.Moulis,
and
I.M.Mavridis
(2006).
The structure of the 2[4Fe-4S] ferredoxin from Pseudomonas aeruginosa at 1.32-A resolution: comparison with other high-resolution structures of ferredoxins and contributing structural features to reduction potential values.
|
| |
J Biol Inorg Chem,
11,
445-458.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
C.E.Ergenekan,
D.Thomas,
J.T.Fischer,
M.L.Tan,
M.K.Eidsness,
C.Kang,
and
T.Ichiye
(2003).
Prediction of reduction potential changes in rubredoxin: a molecular mechanics approach.
|
| |
Biophys J,
85,
2818-2829.
|
|
|
|
|
|
|
K.Chen,
C.A.Bonagura,
G.J.Tilley,
J.P.McEvoy,
Y.S.Jung,
F.A.Armstrong,
C.D.Stout,
and
B.K.Burgess
(2002).
Crystal structures of ferredoxin variants exhibiting large changes in [Fe-S] reduction potential.
|
| |
Nat Struct Biol,
9,
188-192.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
C.G.Schipke,
D.B.Goodin,
D.E.McRee,
and
C.D.Stout
(1999).
Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster.
|
| |
Biochemistry,
38,
8228-8239.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
P.Kyritsis,
R.Kümmerle,
J.G.Huber,
J.Gaillard,
B.Guigliarelli,
C.Popescu,
E.Münck,
and
J.M.Moulis
(1999).
Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxin.
|
| |
Biochemistry,
38,
6335-6345.
|
|
|
|
|
|
|
M.A.Kemper,
H.S.Gao-Sheridan,
B.Shen,
J.L.Duff,
G.J.Tilley,
F.A.Armstrong,
and
B.K.Burgess
(1998).
Delta T 14/Delta D 15 Azotobacter vinelandii ferredoxin I: creation of a new CysXXCysXXCys motif that ligates a [4Fe-4S] cluster.
|
| |
Biochemistry,
37,
12829-12837.
|
|
|
|
|
|
|
W.N.Lanzilotta,
J.Christiansen,
D.R.Dean,
and
L.C.Seefeldt
(1998).
Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenase.
|
| |
Biochemistry,
37,
11376-11384.
|
|
|
|
|
|
|
J.K.Hurley,
A.M.Weber-Main,
M.T.Stankovich,
M.M.Benning,
J.B.Thoden,
J.L.Vanhooke,
H.M.Holden,
Y.K.Chae,
B.Xia,
H.Cheng,
J.L.Markley,
M.Martinez-Júlvez,
C.Gómez-Moreno,
J.L.Schmeits,
and
G.Tollin
(1997).
Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants.
|
| |
Biochemistry,
36,
11100-11117.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
P.D.Swartz,
and
T.Ichiye
(1997).
Protein contributions to redox potentials of homologous rubredoxins: an energy minimization study.
|
| |
Biophys J,
73,
2733-2741.
|
|
|
|
|
|
|
A.Soriano,
D.Li,
S.Bian,
A.Agarwal,
and
J.A.Cowan
(1996).
Factors influencing redox thermodynamics and electron self-exchange for the [Fe4S4] cluster in Chromatium vinosum high potential iron protein: the role of core aromatic residues in defining cluster redox chemistry.
|
| |
Biochemistry,
35,
12479-12486.
|
|
|
|
|
|
|
I.Naud,
C.Meyer,
L.David,
J.Breton,
J.Gaillard,
and
Y.Jouanneau
(1996).
Identification of residues of Rhodobacter capsulatus ferredoxin I important for its interaction with nitrogenase.
|
| |
Eur J Biochem,
237,
399-405.
|
|
|
|
|
|
|
P.D.Swartz,
B.W.Beck,
and
T.Ichiye
(1996).
Structural origins of redox potentials in Fe-S proteins: electrostatic potentials of crystal structures.
|
| |
Biophys J,
71,
2958-2969.
|
|
|
|
|
|
|
P.D.Swartz,
and
T.Ichiye
(1996).
Temperature dependence of the redox potential of rubredoxin from Pyrococcus furiosus: a molecular dynamics study.
|
| |
Biochemistry,
35,
13772-13779.
|
|
|
|
|
|
|
S.Bian,
C.F.Hemann,
R.Hille,
and
J.A.Cowan
(1996).
Characterization of an autoreduction pathway for the [Fe4S4]3+ cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center provide evidence for oxidative degradation via a [Fe3S4] cluster.
|
| |
Biochemistry,
35,
14544-14552.
|
|
|
|
|
|
|
B.Shen,
D.R.Jollie,
T.C.Diller,
C.D.Stout,
P.J.Stephens,
and
B.K.Burgess
(1995).
Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation.
|
| |
Proc Natl Acad Sci U S A,
92,
10064-10068.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
H.Lauble,
and
C.D.Stout
(1995).
Steric and conformational features of the aconitase mechanism.
|
| |
Proteins,
22,
1.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
I.Bertini,
A.Donaire,
B.A.Feinberg,
C.Luchinat,
M.Piccioli,
and
H.Yuan
(1995).
Solution structure of the oxidized 2[4Fe-4S] ferredoxin from Clostridium pasteurianum.
|
| |
Eur J Biochem,
232,
192-205.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
J.N.Butt,
J.Niles,
F.A.Armstrong,
J.Breton,
and
A.J.Thomson
(1994).
Formation and properties of a stable 'high-potential' copper-iron-sulphur cluster in a ferredoxin.
|
| |
Nat Struct Biol,
1,
427-433.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
|
Links
