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Volume 143, Issue 5

flavohaemoglobin (Hmp) reduces cytochrome and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen Free

Abstract

flavohaemoglobin (Hmp) reduced purified mitochondrial cytochrome c aerobically in a reaction that was not substantially inhibited by superoxide dismutase, demonstrating that superoxide anion, the product of O reduction by Hmp, did not contribute markedly to cytochrome reduction. Cytochrome was reduced by Hmp even in the presence of 0⋅ 5 mM CO, when the haem B was locked in the ferrous, low-spin state, demonstrating that electron transfer to cytochrome from NADH was via FAD, not haem. Hmp also reduced the ferrisiderophore complex Fe(III)-hydroxamate K from bv. anaerobically in a CO-insensitive manner, but at low rates and with low affinity for this substrate. The NADH-cytochrome oxidoreductase activity of Hmp was slightly sensitive to the binding and reduction of O at the haem. The of cytochrome reduction fell from 7.1 sin the presence of 0⋅5 mM CO to 5⋅0 sin the presence of 100 μM Owith no significant change in K for cytochrome (6⋅8 to 7⋅3 μM, respectively). O at near-micromolar concentrations diminished cytochrome reduction to a similar extent as did 100 μM O Thus, Hmp acts as a reductase of broad specificity, apparently without involvement of electron transfer via the globin-like haem. These data are consistent with the hypothesis that Hmp could act as an intracellular sensor of O since, in the absence of O electron flux from FAD to other electron acceptors increases. However, the nature of such acceptors is not known and alternative models for O sensing are also considered.

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Keyword(s): Escherichia coli , haemoglobin (bacterial) , Hmp , NADH-cytochrome c oxidoreductase and oxygen sensor
© Society Society for General Microbiology 1997
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1997-05-01
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Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen
Microbiology 143, 1557 (1997); https://doi.org/10.1099/00221287-143-5-1557
/content/journal/micro/10.1099/00221287-143-5-1557
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