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PDBsum entry 2wc1
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Electron transport
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PDB id
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2wc1
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References listed in PDB file
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Key reference
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Title
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Structural and phylogenetic analysis of rhodobacter capsulatus niff: uncovering general features of nitrogen-Fixation (nif)-Flavodoxins.
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Authors
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I.Pérez-Dorado,
A.Bortolotti,
N.Cortez,
J.A.Hermoso.
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Ref.
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Int J Mol Sci, 2013,
14,
1152-1163.
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PubMed id
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Abstract
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Analysis of the crystal structure of NifF from Rhodobacter capsulatus and its
homologues reported so far reflects the existence of unique structural features
in nif flavodoxins: a leucine at the re face of the isoalloxazine, an
eight-residue insertion at the C-terminus of the 50's loop and a remarkable
difference in the electrostatic potential surface with respect to non-nif
flavodoxins. A phylogenetic study on 64 sequences from 52 bacterial species
revealed four clusters, including different functional prototypes, correlating
the previously defined as "short-chain" with the firmicutes
flavodoxins and the "long-chain" with gram-negative species. The
comparison of Rhodobacter NifF structure with other bacterial flavodoxin
prototypes discloses the concurrence of specific features of these functional
electron donors to nitrogenase.
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Secondary reference #1
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Title
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Crystallization of a flavodoxin involved in nitrogen fixation in rhodobacter capsulatus.
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Authors
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I.Pérez-Dorado,
A.Bortolotti,
N.Cortez,
J.A.Hermoso.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
375-377.
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PubMed id
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Secondary reference #2
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Title
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The ferredoxin-Nadp(h) reductase from rhodobacter capsulatus: molecular structure and catalytic mechanism.
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Authors
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I.Nogués,
I.Pérez-Dorado,
S.Frago,
C.Bittel,
S.G.Mayhew,
C.Gómez-Moreno,
J.A.Hermoso,
M.Medina,
N.Cortez,
N.Carrillo.
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Ref.
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Biochemistry, 2005,
44,
11730-11740.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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The oxidant-Responsive diaphorase of rhodobacter capsulatus is a ferredoxin (flavodoxin)-Nadp(h) reductase.
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Authors
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C.Bittel,
L.C.Tabares,
M.Armesto,
N.Carrillo,
N.Cortez.
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Ref.
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FEBS Lett, 2003,
553,
408-412.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. The R. capsulatus genomic region around the fpr
gene. Arrows indicate direction of transcription. The fpr coding
sequence (in black) is located downstream of a gene cluster
which is homologous to a bacterial operon involved in cysteine
biosynthesis [39]. The N-terminal sequence determined on the
purified FPR is highlighted. The 5′ untranslated region
contains canonical −10 and −35 consensus sequences, and
three RegA boxes centered at −80, −128 and −188 (consensus
sequences are bold).
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Figure 4.
Fig. 4. Spectroscopic characterization of R. capsulatus
FPR. For the spectrum at wavelengths below 300 nm, enzyme was
diluted 3-fold. The insets display CD spectra of 0.45 μM FPR
(A) or 9 μM FPR (B) in 5 mM phosphate buffer pH 7.0.
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The above figures are
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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Secondary reference #4
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Title
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Stopped-Flow kinetic studies of low potential electron carriers of the photosynthetic bacterium, Rhodobacter capsulatus: ferredoxin i and niff.
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Authors
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P.C.Hallenbeck,
G.Gennaro.
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Ref.
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Biochim Biophys Acta, 1998,
1365,
435-442.
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PubMed id
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Secondary reference #5
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Title
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Cloning, Characterization, And regulation of niff from rhodobacter capsulatus.
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Authors
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G.Gennaro,
P.Hübner,
U.Sandmeier,
A.F.Yakunin,
P.C.Hallenbeck.
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Ref.
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J Bacteriol, 1996,
178,
3949-3952.
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PubMed id
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Secondary reference #6
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Title
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Purification and properties of a nif-Specific flavodoxin from the photosynthetic bacterium rhodobacter capsulatus.
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Authors
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A.F.Yakunin,
G.Gennaro,
P.C.Hallenbeck.
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Ref.
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J Bacteriol, 1993,
175,
6775-6780.
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PubMed id
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