Purification and properties of NADH-cytochrome o Reductase from vitreoscilla.

Gonzales-Prevatt, Victoria; Webster, D. R.

doi:10.1016/s0021-9258(19)86055-6

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The Ce Region and The Distal Site1

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1984

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Cited by 28 publications

(2 citation statements)

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“…A hypothetical heterodimeric form of VtHb (composed of one heme binding subunit and one NADH-dependent flavoprotein reductase subunit) has been proposed. In this heterodimeric form of VtHb, the protein may conform to a flavoHb-like structural organization, achieving cellular functions similar to those played by the single chain flavoHb isolated from bacteria and yeast [37][38][39].…”

Section: Discussionmentioning

confidence: 99%

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Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp

et al. 1997

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Section: Discussionmentioning

confidence: 99%

“…and partly characterized. This flavoprotein has been proposed to be the natural reducing agent for the heme domain of VtHb [37][38][39].…”

Section: The Ce Region and The Distal Sitementioning

confidence: 99%

Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp

et al. 1997

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Listing of Protein Spectra

Kirschenbaum

1984

Bibliographic Atlas of Protein Spectra in the Ultraviolet and Visible Regions

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Identification of b, c, and d cytochromes in the membrane of Vitreoscilla

Georgiou

Webster

1987

Arch. Microbiol.

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Cytochromes b, c, d, and o were identified by spectroscopic analysis of respiratory membrane fragments from Vitreoscilla sp., strain C1. Carbon monoxide difference spectra of the reduced membranes had absorption maxima at 416, 534, and 571 nm (ascribed to cytochrome o) and 632 nm (cytochrome d). Derivative spectra of the pyridine hemochromogen spectra of the membranes identified the presence of b- and c-type cytochromes in Vitreoscilla. The cyanide binding curve of the membranes was biphasic with dissociation constants of 2.14 mM and 10.7 which were assigned to cytochrome o and cytochrome d, respectively. Membranes bound carbon monoxide with dissociation constant 3.9 microM, which was assigned to cytochrome o. Cytochrome c556 and a NADH-p-iodonitrotetrazolium violet reductase component were partially purified from Vitreoscilla membranes.

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Purification and properties of NADH-cytochrome o Reductase from vitreoscilla.

Cited by 28 publications

References 18 publications

Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp

Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp

Listing of Protein Spectra

Identification of b, c, and d cytochromes in the membrane of Vitreoscilla

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