A reappraisal of the role of the low potential c-type cytochrome (cytochrome c-552) in NADH-dependent nitrite reduction and its relationship with a co-purified NADH oxidase in Escherichia coli K-12

Liu, M

doi:10.1016/0378-1097(81)90120-8

Cited by 6 publications

(9 citation statements)

References 6 publications

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“…Finally, there have been many reports that proteins now known to function physiologically as nitrite reductases can also reduce oxygen (Steenkamp & Peck, 1980;Liu et al, 1981;Timkovich et al, 1982). In contrast, our study has provided the first example of a component of cytochrome oxidase that plays a physiologically significant role in nitrite reduction.…”

Section: Bjapomentioning

confidence: 73%

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb₃fromNeisseria gonorrhoeae

Hopper

Tovell

Cole

2009

FEMS Microbiology Letters

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The CcoP subunit of cytochrome oxidase cbb(3) of Neisseria gonorrhoeae is predicted to include a C-terminal extension in which there is a C-A-A-C-H- motif typical of heme attachment sites in c-type cytochromes. Substitutions of key cysteine and histidine residues of this motif resulted in mutants that grew normally in oxygen-sufficient cultures and reduced oxygen at the same rate as the parent strain. In contrast, after oxygen-limited growth in the presence of nitrite, rates of nitrite reduction were significantly lower than those of the parent, consistent with a role for this third heme-binding domain in electron transfer to the nitrite reductase, AniA, located in the outer membrane. As the mutants were still able to reduce nitrite at approximately 65% of the rate of the parent, there are multiple pathways in the gonococcus for electron transfer to AniA. On the basis of sequence similarity between the C-terminal extension of CcoP and cytochrome c(5), it is proposed that cytochrome c(5) might also transfer electrons across the periplasm from the cytochrome bc(1) complex in the cytoplasmic membrane to AniA in the outer membrane. This is the first example of a cytochrome oxidase component that plays a physiologically significant role in nitrite reduction.

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Section: Bjapomentioning

confidence: 73%

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb₃fromNeisseria gonorrhoeae

Hopper

Tovell

Cole

2009

FEMS Microbiology Letters

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“…NrfA proteins with similar properties have been purified and characterized from many different organisms, e.g. Escherichia coli [8–10], Desulfovibrio desulfuricans [11], Wolinella succinogenes [12–14] and Vibrio fischeri [15,16]. For many years, the NrfA protein was considered to contain six heme c groups, mainly based on absorption and electron paramagnetic resonance (EPR) spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

Enzymology and bioenergetics of respiratory nitrite ammonification

Simon

2002

FEMS Microbiol Rev

348

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Nitrite is widely used by bacteria as an electron acceptor under anaerobic conditions. In respiratory nitrite ammonification an electrochemical proton potential across the membrane is generated by electron transport from a non-fermentable substrate like formate or H(2) to nitrite. The corresponding electron transport chain minimally comprises formate dehydrogenase or hydrogenase, a respiratory quinone and cytochrome c nitrite reductase. The catalytic subunit of the latter enzyme (NrfA) catalyzes nitrite reduction to ammonia without liberating intermediate products. This review focuses on recent progress that has been made in understanding the enzymology and bioenergetics of respiratory nitrite ammonification. High-resolution structures of NrfA proteins from different bacteria have been determined, and many nrf operons sequenced, leading to the prediction of electron transfer pathways from the quinone pool to NrfA. Furthermore, the coupled electron transport chain from formate to nitrite of Wolinella succinogenes has been reconstituted by incorporating the purified enzymes into liposomes. The NrfH protein of W. succinogenes, a tetraheme c-type cytochrome of the NapC/NirT family, forms a stable complex with NrfA in the membrane and serves in passing electrons from menaquinol to NrfA. Proteins similar to NrfH are predicted by open reading frames of several bacterial nrf gene clusters. In gamma-proteobacteria, however, NrfH is thought to be replaced by the nrfBCD gene products. The active site heme c group of NrfA proteins from different bacteria is covalently bound via the cysteine residues of a unique CXXCK motif. The lysine residue of this motif serves as an axial ligand to the heme iron thus replacing the conventional histidine residue. The attachment of the lysine-ligated heme group requires specialized proteins in W. succinogenes and Escherichia coli that are encoded by accessory nrf genes. The proteins predicted by these genes are unrelated in the two bacteria but similar to proteins of the respective conventional cytochrome c biogenesis systems.

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“…Although E. coli contains no homologue of the mitochondrial cytochrome c, it does contain a nitrite reductase which contains this prosthetic group [7,8]. Although E. coli contains no homologue of the mitochondrial cytochrome c, it does contain a nitrite reductase which contains this prosthetic group [7,8].…”

Section: H3c ~ Ch=ch2mentioning

confidence: 99%

“…It is a water-soluble enzyme located in the periplasm, where it cata-393 lyzes the six-electron reduction of nitrite to ammonia [7,8]. It is a water-soluble enzyme located in the periplasm, where it cata-393 lyzes the six-electron reduction of nitrite to ammonia [7,8].…”

Section: Nitrite Reductase (Cytochrome %52)mentioning

confidence: 99%

The cytochromes of Escherichia coli

Gennis

1987

FEMS Microbiology Letters

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Escherichia coli contains numerous heme‐containing proteins when grown either aerobicaly or anaerobically. These cytochrome species are distributed in the cytoplasm, the periplasm, or are bound to the cytoplasmic membrane. They are involved in various physiological functions, including electron transport, oxidative phosphorylation, assimilatory metabolism and detoxification. One dozen unique cytochrome species have been biochemically and/or genetically characterized. They contain one or more of the four heme groups which E. coli is known to produce: protoheme IX, heme c, heme d, and siroheme. The purpose of this articles is to summarize what we know about the structure and function of this collection of heme proteins.

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A reappraisal of the role of the low potential c-type cytochrome (cytochrome c-552) in NADH-dependent nitrite reduction and its relationship with a co-purified NADH oxidase in Escherichia coli K-12

Cited by 6 publications

References 6 publications

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb₃fromNeisseria gonorrhoeae

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb₃fromNeisseria gonorrhoeae

Enzymology and bioenergetics of respiratory nitrite ammonification

The cytochromes of Escherichia coli

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A reappraisal of the role of the low potential c-type cytochrome (cytochrome c-552) in NADH-dependent nitrite reduction and its relationship with a co-purified NADH oxidase in Escherichia coli K-12

Cited by 6 publications

References 6 publications

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb3fromNeisseria gonorrhoeae

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb3fromNeisseria gonorrhoeae

Enzymology and bioenergetics of respiratory nitrite ammonification

The cytochromes of Escherichia coli

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A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb₃fromNeisseria gonorrhoeae

A physiologically significant role in nitrite reduction of the CcoP subunit of the cytochrome oxidasecbb₃fromNeisseria gonorrhoeae