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800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.

The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been
refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact
shifts in the final energy minimization procedure. The protein, composed of 68
amino acids, contains three paramagnetic heme moieties, each with one unpaired
electron. The largely distributed paramagnetism broadens the lines in several
protein parts. The structure is now relatively well resolved all over the
backbone by the use of 1315 meaningful NOEs and 90 pseudocontact shifts. The
statistical analysis of the structure indicates its satisfactory quality. The
protein-fold is quite similar to that of the analogous four-heme cytochromes c3
for those parts which can be considered homologous. The solvent accessibility
and the electrostatic potential surfaces surrounding the three hemes have been
analyzed in terms of their reduction potentials. The resulting magnetic
susceptibility anisotropy data obtained from pseudocontact shifts are analyzed
in terms of structural data.

A Proton-Nmr Investigation Of The Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans

A Proton-Nmr Investigation Of The Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between The Reduced A

Cytochrome C7 From Desulfuromonas Acetoxidans

Solution Structure Determination Of The Fully Oxidized Double Mutant K9-10a Cytochrome C7 From Desulfuromonas Acetoxidans, Mini

Solution Structure Determination Of The Fully Oxidized Double Mutant K9-10a Cytochrome C7 From Desulfuromonas Acetoxidans, Ense

Nmr Structural Characterization Of The Reduction Of Chromium(Vi) To Chromium(Iii) By Cytochrome C7

cytochrome c7 [Desulfuromonas acetoxidans]

RecName: Full=Cytochrome c3; AltName: Full=Cytochrome c551.5; AltName: Full=Cytochrome c7

1H Chemical Shift Assignments for fully oxidized cytochrome c7 from
Desulfuromonas acetoxidans