Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O2-• generating oxidase from human neutrophils

Theodore G. Gabig; Bruce A. Lefker

doi:10.1016/0006-291X(84)91321-4

Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O₂^-_• generating oxidase from human neutrophils

Theodore G. Gabig
, Bruce A. Lefker

Medical Oncology

University of Michigan, Ann Arbor
VA Medical Center

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

The resolved flavoprotein and cytochrome b₅₅₉ components of the NADPH dependent O₂^-_• generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b₅₅₉, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent O₂^-_• generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b₅₅₉, depleted of flavoprotein, demonstrated no measureable NADPH dependent O₂^-_• generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b₅₅₉ was rapidly oxidized by oxygen, as was the cytochrome b₅₅₉ in the intact oxidase.

Original language	English
Pages (from-to)	430-436
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	118
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(84)91321-4
State	Published - Jan 30 1984

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title = "Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O2-• generating oxidase from human neutrophils",

abstract = "The resolved flavoprotein and cytochrome b559 components of the NADPH dependent O2-• generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b559, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent O2-• generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent O2-• generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b559 was rapidly oxidized by oxygen, as was the cytochrome b559 in the intact oxidase.",

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T1 - Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O2-• generating oxidase from human neutrophils

AU - Gabig, Theodore G.

AU - Lefker, Bruce A.

PY - 1984/1/30

Y1 - 1984/1/30

N2 - The resolved flavoprotein and cytochrome b559 components of the NADPH dependent O2-• generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b559, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent O2-• generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent O2-• generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b559 was rapidly oxidized by oxygen, as was the cytochrome b559 in the intact oxidase.

AB - The resolved flavoprotein and cytochrome b559 components of the NADPH dependent O2-• generating oxidase from human neutrophils were the subject of further study. The resolved flavoprotein, depleted of cytochrome b559, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent O2-• generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent O2-• generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome b559 was rapidly oxidized by oxygen, as was the cytochrome b559 in the intact oxidase.

UR - https://www.scopus.com/pages/publications/0021773224

U2 - 10.1016/0006-291X(84)91321-4

DO - 10.1016/0006-291X(84)91321-4

M3 - Article

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AN - SCOPUS:0021773224

SN - 0006-291X

VL - 118

SP - 430

EP - 436

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Catalytic properties of the resolved flavoprotein and cytochrome B components of the NADPH dependent O₂^-_• generating oxidase from human neutrophils

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