Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 8 14:33:55 2011

Proceedings of the National Academy of Sciences of the United States of America
Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.

Solution Structure Of Reduced Clostridium Pasteurianum Rubredoxin, Nmr, 20 Structures

X-Ray Crystal Structure Of Oxidized Rubredoxin

X-Ray Crystal Structure Of Reduced Rubredoxin

Rubredoxin (zn-substituted) At 1.2 Angstroms Resolution

Rubredoxin (Oxidized, Fe(Iii)) At 1.1 Angstroms Resolution

Crystal Structure Of The Ccr5 Chemokine Receptor

rubredoxin [Clostridium pasteurianum DSM 525 = ATCC 6013]

Rubredoxin domain containing protein [Clostridium pasteurianum DSM 525 = ATCC 6013]

RecName: Full=Rubredoxin; Short=Rd [Clostridium pasteurianum]

15N hyperfine shifts assignment for rubredoxin (V8G)from Clostridium pasteurianum in the reduced state

The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent system for testing ideas concerning the ways in which a protein sequence of an iron-sulfur protein can modulate the reduction potential of the active site iron. Mutations at two residues (valine-8 and valine-44) are known to affect the reduction potential of CpRd. We report nitrogen-15 NMR spectroscopic results that have allowed us to determine with unprecedented accuracy the lengths (and therefore the strengths) of all six key hydrogen bonds between protein backbone amides and the sulfur atoms of the four cysteine residues that ligate the iron in the oxidized and reduced forms of wild-type CpRd and nine mutants (V44G, V44A, V44I, V44L, V8G, V8A, V8I, V8L and V8G/V44G). The lengths (or strengths) of the hydrogen bonds are inferred from the level of trans-hydrogen-bond electron spin delocalization from the iron atom. The aggregate lengths of these six hydrogen bonds, as reported by the electron spin delocalization effect on the nitrogen-15 chemical shifts, are shorter in both oxidation states in mutants with higher reduction potential than in those with lower reduction potential, and the differences in the aggregate hydrogen bond strengths upon reduction of CpRd correlate linearly with the published reduction potentials for the 10 proteins, which span 126 mV. Sequence effects on the reduction potential can be explained fully, in the case of these CpRd variants, by their effects on hydrogen bonds.
Changes in hydrogen bond strengths explain variations in the reduction potentials of a series of rubredoxin mutants

ubredoxin (V8A) from Clostridium pasteurianum in the oxidized state

ubredoxin (V8A) from Clostridium pasteurianum in the reduced state

wild-type rubredoxin from Clostridium pasteurianum in the reduceded state

rubredoxin (V8G) from Clostridium pasteurianum in the oxidized state

ubredoxin (V8G) from Clostridium pasteurianum in the reduced state

ubredoxin (V8G/V44G) from Clostridium pasteurianum in the oxidized state

ubredoxin (V8G/V44G) from Clostridium pasteurianum in the reduced state

ubredoxin (V8I) from Clostridium pasteurianum in the oxidized state

ubredoxin (V8I) from Clostridium pasteurianum in the reduced state

ubredoxin (V8L) from Clostridium pasteurianum in the oxidized state

ubredoxin (V8L) from Clostridium pasteurianum in the reduced state

rubredoxin (V44A) from Clostridium pasteurianum in the oxidized state

rubredoxin (V44A) from Clostridium pasteurianum in the reduced state

rubredoxin (V44G) from Clostridium pasteurianum in the oxidized state

rubredoxin (V44G) from Clostridium pasteurianum in the reduced state

rubredoxin (V44I) from Clostridium pasteurianum in the oxidized state

rubredoxin (V44I) from Clostridium pasteurianum in the reduced state

rubredoxin (V44L) from Clostridium pasteurianum in the oxidized state

rubredoxin (V44L) from Clostridium pasteurianum in the reduced state