Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

Nong Liang; A. Grant Mauk; Gary J. Pielak; Jeanette A. Johnson; Michael Smith; Brian M. Hoffman

doi:10.1126/science.2832950

Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

Nong Liang^*, A. Grant Mauk, Gary J. Pielak, Jeanette A. Johnson, Michael Smith, Brian M. Hoffman

^*Corresponding author for this work

Chemistry

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Abstract

Yeast iso-l-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)⁺,Fe^IICc] converts to [ZnCcP,Fe^IIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by Fe^IICc subsequent to its formation from Fe^IIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is ∼10⁴ slower at ∼0°C than for the two variants with aromatic residues.

Original language	English (US)
Pages (from-to)	311-313
Number of pages	3
Journal	Science
Volume	240
Issue number	4850
DOIs	https://doi.org/10.1126/science.2832950
State	Published - 1988

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title = "Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c",

abstract = "Yeast iso-l-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by {"}gating{"} through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is ∼104 slower at ∼0°C than for the two variants with aromatic residues.",

author = "Nong Liang and Mauk, {A. Grant} and Pielak, {Gary J.} and Johnson, {Jeanette A.} and Michael Smith and Hoffman, {Brian M.}",

year = "1988",

doi = "10.1126/science.2832950",

language = "English (US)",

volume = "240",

pages = "311--313",

journal = "Science",

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publisher = "American Association for the Advancement of Science",

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TY - JOUR

T1 - Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

AU - Liang, Nong

AU - Mauk, A. Grant

AU - Pielak, Gary J.

AU - Johnson, Jeanette A.

AU - Smith, Michael

AU - Hoffman, Brian M.

PY - 1988

Y1 - 1988

N2 - Yeast iso-l-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is ∼104 slower at ∼0°C than for the two variants with aromatic residues.

AB - Yeast iso-l-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is ∼104 slower at ∼0°C than for the two variants with aromatic residues.

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ER -

Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

Abstract

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