Long-Range Electron Transfer at Fixed and Known Distance within Protein Complexes

S. E. Peterson-Kennedy; J. L. McGourty; P. S. Ho; C. J. Sutoris; N. Liang; H. Zemel; N. V. Blough; E. Margoliash; B. M. Hoffman

doi:10.1016/0010-8545(85)80046-1

Long-Range Electron Transfer at Fixed and Known Distance within Protein Complexes

S. E. Peterson-Kennedy^*, J. L. McGourty, P. S. Ho, C. J. Sutoris, N. Liang, H. Zemel, N. V. Blough, E. Margoliash, B. M. Hoffman

^*Corresponding author for this work

Chemistry

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Abstract

We have used zinc-substituted hemoproteins to study long-range electron transfer between redox centers at fixed and known distances. The photo-excited zinc triplet state in one subunit of the α₁-β₂ electron transfer complex of [Zn,Fe] hybrid hemoglobin transfers an electron to its partner aquoferriheme subunit at a rate, k_t=100 s^-1. The temperature dependence of this electron transfer from 77K to 313K is indicative of non-adiabatic electron tunnelling in which the accompanying nuclear rearrangements proceed by nuclear tunnelling. For the complex between zinc-substituted yeast cytochrome c peroxidase (CCP) and native yeast cytochrome c, electron transfer occurs at a rate, k_t=138 s^-1, compared to k_t = 17 s^-1 in the complex between the yeast enzyme and horse cyt c. The difference demonstrates the species specificity involved in physiological electron transfer. Oxidation of ferroporphyrin by the zinc porphyrin radical is more rapid, and, for the yeast cytochrome, occurs with a rate, k_h ∼ 10⁴ s^-1.

Original language	English (US)
Pages (from-to)	125-133
Number of pages	9
Journal	Coordination Chemistry Reviews
Volume	64
Issue number	C
DOIs	https://doi.org/10.1016/0010-8545(85)80046-1
State	Published - May 1985

Funding

This work has been supported by NIH Grant HL13531'and NSF Grant PCM 76-81304. It has been encouraged by stimulating discussions with H.B. Gray, S. Iseid, G. McLendon, J. Miller, M.A. Ratner, and R.P. Van Duyne.

ASJC Scopus subject areas

General Chemistry
Physical and Theoretical Chemistry
Inorganic Chemistry
Materials Chemistry

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10.1016/0010-8545(85)80046-1

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title = "Long-Range Electron Transfer at Fixed and Known Distance within Protein Complexes",

abstract = "We have used zinc-substituted hemoproteins to study long-range electron transfer between redox centers at fixed and known distances. The photo-excited zinc triplet state in one subunit of the α1-β2 electron transfer complex of [Zn,Fe] hybrid hemoglobin transfers an electron to its partner aquoferriheme subunit at a rate, kt=100 s-1. The temperature dependence of this electron transfer from 77K to 313K is indicative of non-adiabatic electron tunnelling in which the accompanying nuclear rearrangements proceed by nuclear tunnelling. For the complex between zinc-substituted yeast cytochrome c peroxidase (CCP) and native yeast cytochrome c, electron transfer occurs at a rate, kt=138 s-1, compared to kt = 17 s-1 in the complex between the yeast enzyme and horse cyt c. The difference demonstrates the species specificity involved in physiological electron transfer. Oxidation of ferroporphyrin by the zinc porphyrin radical is more rapid, and, for the yeast cytochrome, occurs with a rate, kh ∼ 104 s-1.",

author = "Peterson-Kennedy, {S. E.} and McGourty, {J. L.} and Ho, {P. S.} and Sutoris, {C. J.} and N. Liang and H. Zemel and Blough, {N. V.} and E. Margoliash and Hoffman, {B. M.}",

note = "Funding Information: This work has been supported by NIH Grant HL13531'and NSF Grant PCM 76-81304. It has been encouraged by stimulating discussions with H.B. Gray, S. Iseid, G. McLendon, J. Miller, M.A. Ratner, and R.P. Van Duyne.",

year = "1985",

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doi = "10.1016/0010-8545(85)80046-1",

language = "English (US)",

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pages = "125--133",

journal = "Coordination Chemistry Reviews",

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T1 - Long-Range Electron Transfer at Fixed and Known Distance within Protein Complexes

AU - Peterson-Kennedy, S. E.

AU - McGourty, J. L.

AU - Ho, P. S.

AU - Sutoris, C. J.

AU - Liang, N.

AU - Zemel, H.

AU - Blough, N. V.

AU - Margoliash, E.

AU - Hoffman, B. M.

N1 - Funding Information: This work has been supported by NIH Grant HL13531'and NSF Grant PCM 76-81304. It has been encouraged by stimulating discussions with H.B. Gray, S. Iseid, G. McLendon, J. Miller, M.A. Ratner, and R.P. Van Duyne.

PY - 1985/5

Y1 - 1985/5

N2 - We have used zinc-substituted hemoproteins to study long-range electron transfer between redox centers at fixed and known distances. The photo-excited zinc triplet state in one subunit of the α1-β2 electron transfer complex of [Zn,Fe] hybrid hemoglobin transfers an electron to its partner aquoferriheme subunit at a rate, kt=100 s-1. The temperature dependence of this electron transfer from 77K to 313K is indicative of non-adiabatic electron tunnelling in which the accompanying nuclear rearrangements proceed by nuclear tunnelling. For the complex between zinc-substituted yeast cytochrome c peroxidase (CCP) and native yeast cytochrome c, electron transfer occurs at a rate, kt=138 s-1, compared to kt = 17 s-1 in the complex between the yeast enzyme and horse cyt c. The difference demonstrates the species specificity involved in physiological electron transfer. Oxidation of ferroporphyrin by the zinc porphyrin radical is more rapid, and, for the yeast cytochrome, occurs with a rate, kh ∼ 104 s-1.

AB - We have used zinc-substituted hemoproteins to study long-range electron transfer between redox centers at fixed and known distances. The photo-excited zinc triplet state in one subunit of the α1-β2 electron transfer complex of [Zn,Fe] hybrid hemoglobin transfers an electron to its partner aquoferriheme subunit at a rate, kt=100 s-1. The temperature dependence of this electron transfer from 77K to 313K is indicative of non-adiabatic electron tunnelling in which the accompanying nuclear rearrangements proceed by nuclear tunnelling. For the complex between zinc-substituted yeast cytochrome c peroxidase (CCP) and native yeast cytochrome c, electron transfer occurs at a rate, kt=138 s-1, compared to kt = 17 s-1 in the complex between the yeast enzyme and horse cyt c. The difference demonstrates the species specificity involved in physiological electron transfer. Oxidation of ferroporphyrin by the zinc porphyrin radical is more rapid, and, for the yeast cytochrome, occurs with a rate, kh ∼ 104 s-1.

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JO - Coordination Chemistry Reviews

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ER -

Long-Range Electron Transfer at Fixed and Known Distance within Protein Complexes

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