Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3

Andrew W. Munro; J. Gordon Lindsay; John R. Coggins; Sharon M. Kelly; Nicholas C. Price

doi:10.1016/0014-5793(94)80609-8

Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3

Andrew W. Munro
, J. Gordon Lindsay
, John R. Coggins
, Sharon M. Kelly
, Nicholas C. Price

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

Abstract

The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain. © 1994.

Original language	English
Pages (from-to)	70-74
Number of pages	4
Journal	FEBS Letters
Volume	343
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(94)80609-8
Publication status	Published - 18 Apr 1994

Keywords

Circular dichroism
Cytochrome P-450 BM3
Domain interaction
Electron transfer
Haem environment

Access to Document

10.1016/0014-5793(94)80609-8

Cite this

@article{5c18b406abb8417b96eebab85f0dcb73,

title = "Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3",

abstract = "The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain. {\textcopyright} 1994.",

keywords = "Circular dichroism, Cytochrome P-450 BM3, Domain interaction, Electron transfer, Haem environment",

author = "Munro, \{Andrew W.\} and Lindsay, \{J. Gordon\} and Coggins, \{John R.\} and Kelly, \{Sharon M.\} and Price, \{Nicholas C.\}",

year = "1994",

month = apr,

day = "18",

doi = "10.1016/0014-5793(94)80609-8",

language = "English",

volume = "343",

pages = "70--74",

journal = "FEBS Letters",

publisher = "John Wiley \& Sons Ltd",

number = "1",

}

TY - JOUR

T1 - Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3

AU - Munro, Andrew W.

AU - Lindsay, J. Gordon

AU - Coggins, John R.

AU - Kelly, Sharon M.

AU - Price, Nicholas C.

PY - 1994/4/18

Y1 - 1994/4/18

N2 - The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain. © 1994.

AB - The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain. © 1994.

KW - Circular dichroism

KW - Cytochrome P-450 BM3

KW - Domain interaction

KW - Electron transfer

KW - Haem environment

U2 - 10.1016/0014-5793(94)80609-8

DO - 10.1016/0014-5793(94)80609-8

M3 - Article

C2 - 8163021

VL - 343

SP - 70

EP - 74

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3

Abstract

Keywords

Access to Document

Fingerprint

Cite this