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. 1985 Oct;164(1):316-20.
doi: 10.1128/jb.164.1.316-320.1985.

Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas

D J Klemm, L L Barton

Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas

D J Klemm et al. J Bacteriol. 1985 Oct.

Abstract

The anaerobic oxidation of protoporphyrinogen to protoporphyrin was demonstrated in extracts of Desulfovibrio gigas. Protoporphyrin formation occurred in the presence of nitrite, hydroxylamine, sulfite, thiosulfate, ATP plus sulfate, NAD+, NADP+, flavin adenine dinucleotide, flavin mononucleotide, fumarate, 2,6-dichlorophenol-indophenol, methyl viologen, and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide. With dialyzed cell extracts, highest activities were observed with sulfite, NAD+, and NADP+ as electron acceptors. The enzyme for protoporphyrinogen oxidation was localized in the membrane of D. gigas and displayed optimal activity at pH 7.3 and 28 degrees C.

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