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• W2056588828 abstract "Protoporphyrinogen oxidase (PPO, EC 1.3.3.4) catalyzes the six-electron oxidation of protoporphyrinogen IX to the fully conjugated protoporphyrin IX. Eukaryotes and Gram-positive bacteria possess an oxygen-dependent, FAD-containing enzyme for this step, while the majority of Gram-negative bacteria lack this oxygen-dependent PPO. In Escherichia coli, PPO activity is known to be linked to respiration and the quinone pool. In E. coli SASX38, the knockout of hemG causes a loss of measurable PPO activity. HemG is a small soluble protein typical of long chain flavodoxins. Herein, purified recombinant HemG was shown to be capable of a menadione-dependent conversion of protoporphyrinogen IX to protoporphyrin IX. Electrochemical analysis of HemG revealed similarities to other flavodoxins. Interestingly, HemG, a member of a class of the long chain flavodoxin family that is unique to the γ-proteobacteria, possesses a 22-residue sequence that, when transferred into E. coli flavodoxin A, produces a chimera that will complement an E. coli hemG mutant, indicating that this region confers PPO activity to the flavodoxin. These findings reveal a previously unidentified class of PPO enzymes that do not utilize oxygen as an electron acceptor, thereby allowing γ-proteobacteria to synthesize heme in both aerobic and anaerobic environments." @default.
• W2056588828 created "2016-06-24" @default.
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• W2056588828 date "2009-07-07" @default.
• W2056588828 modified "2023-10-12" @default.
• W2056588828 title "Identification of <i>Escherichia coli</i> HemG as a Novel, Menadione-Dependent Flavodoxin with Protoporphyrinogen Oxidase Activity" @default.
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• W2056588828 doi "https://doi.org/10.1021/bi900850y" @default.
• W2056588828 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2749469" @default.
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