Enzymatic and electron transfer activities in crystalline protein complexes

A. Merli; Ditlev Egeskov Brodersen; B. Morini; Z.-W. Chen; R. C. E. Durley; F. Scott Mathews; V. L. Davidson; G. L. Rossi

Enzymatic and electron transfer activities in crystalline protein complexes

A. Merli, Ditlev Egeskov Brodersen, B. Morini, Z.-W. Chen, R. C. E. Durley, F. Scott Mathews, V. L. Davidson, G. L. Rossi

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

47 Citationer (Scopus)

Abstract

Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c551i via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme.

Originalsprog	Engelsk
Tidsskrift	Journal of Biological Chemistry
Vol/bind	271
Nummer	16
Sider (fra-til)	9177-9180
ISSN	0021-9258
Status	Udgivet - 1996
Udgivet eksternt	Ja

Citationsformater

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title = "Enzymatic and electron transfer activities in crystalline protein complexes",

abstract = "Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c551i via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme.",

author = "A. Merli and Brodersen, {Ditlev Egeskov} and B. Morini and Z.-W. Chen and Durley, {R. C. E.} and {Scott Mathews}, F. and Davidson, {V. L.} and Rossi, {G. L.}",

year = "1996",

language = "English",

volume = "271",

pages = "9177--9180",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

number = "16",

}

TY - JOUR

T1 - Enzymatic and electron transfer activities in crystalline protein complexes

AU - Merli, A.

AU - Brodersen, Ditlev Egeskov

AU - Morini, B.

AU - Chen, Z.-W.

AU - Durley, R. C. E.

AU - Scott Mathews, F.

AU - Davidson, V. L.

AU - Rossi, G. L.

PY - 1996

Y1 - 1996

N2 - Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c551i via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme.

AB - Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c551i via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme.

M3 - Journal article

SN - 0021-9258

VL - 271

SP - 9177

EP - 9180

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 16

ER -

Enzymatic and electron transfer activities in crystalline protein complexes

Abstract

Fingeraftryk

Citationsformater