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Article

Pulsed EPR investigations of the Mo(V) centers of the R55Q and R55M variants of sulfite dehydrogenase from Starkeya novella.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 May 2010

Rapson Trevor D, Astashkin Andrei V, Johnson-Winters Kayunta, Bernhardt Paul V, Kappler Ulrike, Raitsimring Arnold M, Enemark John H

Abstract excerpt

Continuous-wave and pulsed electron paramagnetic resonance (EPR) spectroscopy have been used to characterize two variants of bacterial sulfite dehydrogenase (SDH) from Starkeya novella in which the conserved active-site arginine residue (R55) is replaced by a neutral amino acid residue. Substitution by the hydrophobic methionine residue (SDH(R55M)) has essentially no effect on the pH dependence of the EPR...

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Identifiers

PMID: 20084533
DOI: 10.1007/s00775-009-0619-0
PMCID: PMC2875948

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