pH dependence of the tryptophan fluorescence in cytochrome c oxidase: further evidence for a redox-linked conformational change associated with CuA

Robert A. Copeland; Paul A. Smith; Sunney I. Chan

doi:10.1021/bi00410a004

pH dependence of the tryptophan fluorescence in cytochrome c oxidase: further evidence for a redox-linked conformational change associated with CuA

Biochemistry ◽

10.1021/bi00410a004 ◽

1988 ◽

Vol 27 (10) ◽

pp. 3552-3555 ◽

Cited By ~ 10

Author(s):

Robert A. Copeland ◽

Paul A. Smith ◽

Sunney I. Chan

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Ph Dependence ◽

Tryptophan Fluorescence

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Cytochrome c oxidase exhibits a rapid conformational change upon reduction of CuA: a tryptophan fluorescence study

Biochemistry ◽

10.1021/bi00397a017 ◽

1987 ◽

Vol 26 (23) ◽

pp. 7311-7316 ◽

Cited By ~ 38

Author(s):

Robert A. Copeland ◽

Paul A. Smith ◽

Sunney I. Chan

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Tryptophan Fluorescence ◽

Fluorescence Study

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Conformational change due to reduction of cytochrome-c oxidase in lauryl maltoside: picosecond time-resolved tryptophan fluorescence studies on the native and heat modified enzyme

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(94)90189-9 ◽

1994 ◽

Vol 1209 (2) ◽

pp. 227-237 ◽

Cited By ~ 10

Author(s):

Tapan Kanti Das ◽

Shyamalava Mazumdar

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Tryptophan Fluorescence ◽

Time Resolved ◽

Fluorescence Studies ◽

Modified Enzyme

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Erratum to ‘conformational change due to reduction of cytochrome-c oxidase in lauryl maltoside: picosecond time-resolved tryptophan fluorescence studies on the native and heat modified enzyme’ [Biochim. Biophys. Acta 1209 (1994) 227–237]

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(95)00027-r ◽

1995 ◽

Vol 1249 (2) ◽

pp. 205 ◽

Cited By ~ 1

Author(s):

Tapan Kanti Das ◽

Shyamalava Mazumdar

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Tryptophan Fluorescence ◽

Time Resolved ◽

Fluorescence Studies ◽

Modified Enzyme

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Intrinsic uncoupling in proton-pumping cytochrome c oxidase: pH dependence of cytochrome c oxidation in coupled and uncoupled phospholipid vesicles

Biochemistry ◽

10.1021/bi00434a007 ◽

1989 ◽

Vol 28 (8) ◽

pp. 3156-3160 ◽

Cited By ~ 19

Author(s):

Brigitta Maison-Peteri ◽

Bo G. Malmstroem

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Ph Dependence ◽

Proton Pumping ◽

Phospholipid Vesicles

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Fourier-transform infrared study of cyanide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: implication of the redox-linked conformational change at the binuclear site. [Erratum to document cited in CA118(5):35099w]

Biochemistry ◽

10.1021/bi00086a038 ◽

1993 ◽

Vol 32 (35) ◽

pp. 9262-9262

Author(s):

Motonari Tsubaki

Keyword(s):

Fourier Transform ◽

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Fourier Transform Infrared ◽

Infrared Study ◽

Bovine Heart ◽

Cyanide Binding

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Fourier-transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: new evidence for a redox-linked conformational change at the binuclear site

Biochemistry ◽

10.1021/bi00052a023 ◽

1993 ◽

Vol 32 (1) ◽

pp. 174-182 ◽

Cited By ~ 23

Author(s):

Motonari Tsubaki ◽

Shinya Yoshikawa

Keyword(s):

Fourier Transform ◽

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Fourier Transform Infrared ◽

Infrared Study ◽

Bovine Heart ◽

New Evidence ◽

Azide Binding

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Cytochrome c oxidase depleted of subunit III: proton-pumping, respiratory control, and pH dependence of the midpoint potential of cytochrome a

Journal of Inorganic Biochemistry ◽

10.1016/0162-0134(85)85046-7 ◽

1985 ◽

Vol 23 (3-4) ◽

pp. 357-364 ◽

Cited By ~ 24

Author(s):

Debra A. Thompson ◽

Linda Gregory ◽

Shelagh Ferguson-Miller

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Ph Dependence ◽

Respiratory Control ◽

Proton Pumping ◽

Midpoint Potential ◽

Subunit Iii

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Difference FT-IR for examination of conformational change in protein potion of bovine heart cytochrome c oxidase.

Seibutsu Butsuri ◽

10.2142/biophys.40.s44_1 ◽

2000 ◽

Vol 40 (supplement) ◽

pp. S44

Author(s):

M. Mochizuki ◽

S. Yoshikawa

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Bovine Heart ◽

Ft Ir

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Reduction of CuA induces a conformational change in cytochrome c oxidase from Paracoccus denitrificans

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/s0005-2728(09)91016-7 ◽

1992 ◽

Vol 1098 (3) ◽

pp. 343-350 ◽

Cited By ~ 12

Author(s):

Tuomas Haltia

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Conformational Change ◽

Paracoccus Denitrificans

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The pH dependence of cytochrome a conformation in cytochrome c oxidase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54371-4 ◽

1991 ◽

Vol 266 (35) ◽

pp. 23916-23920

Author(s):

N. Ishibe ◽

S.R. Lynch ◽

R.A. Copeland

Keyword(s):

Cytochrome C ◽

Cytochrome C Oxidase ◽

Ph Dependence

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