Generation of Superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators

Vasilij Koshkin; Edgar Pick

doi:10.1016/0014-5793(93)81039-3

Generation of Superoxide by purified and relipidated cytochrome b₅₅₉ in the absence of cytosolic activators

Vasilij Koshkin, Edgar Pick^*

^*Corresponding author for this work

Clinical Microbiology and Immunology

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

Abstract

Purified cytochrome b₅₅₉ from guinea pig macrophages was relipidated with several phospholipid mixtures. Relipidated cytochrome b₅₅₉ was found capable of NADPH-dependent Superoxide (O₂^-) production in the absence of the cytosolic components of the NADPH oxidase complex. The rate of O₂^- generation by cytochrome b₅₅₉ varied with the type of phospholipid utilized for relipidation, was absolutely dependent on exogenous FAD, and was enhanced by a critical concentration of anionic amphiphile. It is demonstrated that exogenous FAD acts by binding to cytochrome b₅₅₉. These results provide firm experimental evidence for the proposal that cytochrome b₅₅₉ comprises the complete electron transporting apparatus of the O₂^- forming NADPH oxidase and that the cytosolic components function merely as activators.

Original language	English
Pages (from-to)	57-62
Number of pages	6
Journal	FEBS Letters
Volume	327
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(93)81039-3
State	Published - 19 Jul 1993

Keywords

Cytochrome b
FAD
NADPH oxidase
Phosphatidic acid
Phospholipid
Superoxide

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10.1016/0014-5793(93)81039-3

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title = "Generation of Superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators",

abstract = "Purified cytochrome b559 from guinea pig macrophages was relipidated with several phospholipid mixtures. Relipidated cytochrome b559 was found capable of NADPH-dependent Superoxide (O2-) production in the absence of the cytosolic components of the NADPH oxidase complex. The rate of O2- generation by cytochrome b559 varied with the type of phospholipid utilized for relipidation, was absolutely dependent on exogenous FAD, and was enhanced by a critical concentration of anionic amphiphile. It is demonstrated that exogenous FAD acts by binding to cytochrome b559. These results provide firm experimental evidence for the proposal that cytochrome b559 comprises the complete electron transporting apparatus of the O2- forming NADPH oxidase and that the cytosolic components function merely as activators.",

keywords = "Cytochrome b, FAD, NADPH oxidase, Phosphatidic acid, Phospholipid, Superoxide",

author = "Vasilij Koshkin and Edgar Pick",

note = "Funding Information: Acknowledgemenrs~Th is study was supported by grants from the Israel Academy of Sciences and Humanities; the Israel Cancer Research Fund; a donation from Mr. and Mrs. J. Salzman, Mr. and Mrs. L. Randall and Mr. and Mrs. J. Garbell and the David and Natalie Roberts Chair m Immunopharmacology. We thank Ms. Judith Rap-oport for the excellent typing of the manuscript.",

year = "1993",

month = jul,

day = "19",

doi = "10.1016/0014-5793(93)81039-3",

language = "אנגלית",

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pages = "57--62",

journal = "FEBS Letters",

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T1 - Generation of Superoxide by purified and relipidated cytochrome b559 in the absence of cytosolic activators

AU - Koshkin, Vasilij

AU - Pick, Edgar

N1 - Funding Information: Acknowledgemenrs~Th is study was supported by grants from the Israel Academy of Sciences and Humanities; the Israel Cancer Research Fund; a donation from Mr. and Mrs. J. Salzman, Mr. and Mrs. L. Randall and Mr. and Mrs. J. Garbell and the David and Natalie Roberts Chair m Immunopharmacology. We thank Ms. Judith Rap-oport for the excellent typing of the manuscript.

PY - 1993/7/19

Y1 - 1993/7/19

N2 - Purified cytochrome b559 from guinea pig macrophages was relipidated with several phospholipid mixtures. Relipidated cytochrome b559 was found capable of NADPH-dependent Superoxide (O2-) production in the absence of the cytosolic components of the NADPH oxidase complex. The rate of O2- generation by cytochrome b559 varied with the type of phospholipid utilized for relipidation, was absolutely dependent on exogenous FAD, and was enhanced by a critical concentration of anionic amphiphile. It is demonstrated that exogenous FAD acts by binding to cytochrome b559. These results provide firm experimental evidence for the proposal that cytochrome b559 comprises the complete electron transporting apparatus of the O2- forming NADPH oxidase and that the cytosolic components function merely as activators.

AB - Purified cytochrome b559 from guinea pig macrophages was relipidated with several phospholipid mixtures. Relipidated cytochrome b559 was found capable of NADPH-dependent Superoxide (O2-) production in the absence of the cytosolic components of the NADPH oxidase complex. The rate of O2- generation by cytochrome b559 varied with the type of phospholipid utilized for relipidation, was absolutely dependent on exogenous FAD, and was enhanced by a critical concentration of anionic amphiphile. It is demonstrated that exogenous FAD acts by binding to cytochrome b559. These results provide firm experimental evidence for the proposal that cytochrome b559 comprises the complete electron transporting apparatus of the O2- forming NADPH oxidase and that the cytosolic components function merely as activators.

KW - Cytochrome b

KW - FAD

KW - NADPH oxidase

KW - Phosphatidic acid

KW - Phospholipid

KW - Superoxide

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DO - 10.1016/0014-5793(93)81039-3

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AN - SCOPUS:0027326249

SN - 0014-5793

VL - 327

SP - 57

EP - 62

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Generation of Superoxide by purified and relipidated cytochrome b₅₅₉ in the absence of cytosolic activators

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Keywords

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