Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase

Yoshinori Naruta, Takao Sasaki, Fumito Tani, Yoishimitsu Tachi, Nobuo Kawato, Nobuhumi Nakamura

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Tri(2-pyridylmethyl)amineCu complex-linked iron meso-tetraphenylporphyine derivatives were prepared to model the active site of cytochrome c oxidase. Exposure to oxygen converted the reduced forms of the complexes to the corresponding stable μ-peroxo species in spite of the presence of three coordination sites, two on the heme and one on the Cu. The oxy forms were characterized spectroscopically. Kinetic analyses of the oxygenation reactions of the reduced forms suggests that preferential O2 binding occurs at the Cu site over the heme. This mechanism is also supported by examination of the redox potentials of the two metal ions. Since the peroxy complexes of the models exhibit a structure similar to that of the previously reported fully-oxidized form, the relevance of the model chemistry to the enzyme reaction is discussed.

Original languageEnglish
Pages (from-to)239-246
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume83
Issue number4
DOIs
Publication statusPublished - Jan 1 2001

Fingerprint

Electron Transport Complex IV
Heme
Catalytic Domain
Oxygen
Oxidation-Reduction
Oxygenation
Iron
Metals
Ions
Metal ions
Enzymes
Derivatives
Kinetics

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

Cite this

Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase. / Naruta, Yoshinori; Sasaki, Takao; Tani, Fumito; Tachi, Yoishimitsu; Kawato, Nobuo; Nakamura, Nobuhumi.

In: Journal of Inorganic Biochemistry, Vol. 83, No. 4, 01.01.2001, p. 239-246.

Research output: Contribution to journalArticle

Naruta, Yoshinori ; Sasaki, Takao ; Tani, Fumito ; Tachi, Yoishimitsu ; Kawato, Nobuo ; Nakamura, Nobuhumi. / Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase. In: Journal of Inorganic Biochemistry. 2001 ; Vol. 83, No. 4. pp. 239-246.
@article{6ef09c4ff1d7417fb84fa7f7e6d33c17,
title = "Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase",
abstract = "Tri(2-pyridylmethyl)amineCu complex-linked iron meso-tetraphenylporphyine derivatives were prepared to model the active site of cytochrome c oxidase. Exposure to oxygen converted the reduced forms of the complexes to the corresponding stable μ-peroxo species in spite of the presence of three coordination sites, two on the heme and one on the Cu. The oxy forms were characterized spectroscopically. Kinetic analyses of the oxygenation reactions of the reduced forms suggests that preferential O2 binding occurs at the Cu site over the heme. This mechanism is also supported by examination of the redox potentials of the two metal ions. Since the peroxy complexes of the models exhibit a structure similar to that of the previously reported fully-oxidized form, the relevance of the model chemistry to the enzyme reaction is discussed.",
author = "Yoshinori Naruta and Takao Sasaki and Fumito Tani and Yoishimitsu Tachi and Nobuo Kawato and Nobuhumi Nakamura",
year = "2001",
month = "1",
day = "1",
doi = "10.1016/S0162-0134(00)00170-7",
language = "English",
volume = "83",
pages = "239--246",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase

AU - Naruta, Yoshinori

AU - Sasaki, Takao

AU - Tani, Fumito

AU - Tachi, Yoishimitsu

AU - Kawato, Nobuo

AU - Nakamura, Nobuhumi

PY - 2001/1/1

Y1 - 2001/1/1

N2 - Tri(2-pyridylmethyl)amineCu complex-linked iron meso-tetraphenylporphyine derivatives were prepared to model the active site of cytochrome c oxidase. Exposure to oxygen converted the reduced forms of the complexes to the corresponding stable μ-peroxo species in spite of the presence of three coordination sites, two on the heme and one on the Cu. The oxy forms were characterized spectroscopically. Kinetic analyses of the oxygenation reactions of the reduced forms suggests that preferential O2 binding occurs at the Cu site over the heme. This mechanism is also supported by examination of the redox potentials of the two metal ions. Since the peroxy complexes of the models exhibit a structure similar to that of the previously reported fully-oxidized form, the relevance of the model chemistry to the enzyme reaction is discussed.

AB - Tri(2-pyridylmethyl)amineCu complex-linked iron meso-tetraphenylporphyine derivatives were prepared to model the active site of cytochrome c oxidase. Exposure to oxygen converted the reduced forms of the complexes to the corresponding stable μ-peroxo species in spite of the presence of three coordination sites, two on the heme and one on the Cu. The oxy forms were characterized spectroscopically. Kinetic analyses of the oxygenation reactions of the reduced forms suggests that preferential O2 binding occurs at the Cu site over the heme. This mechanism is also supported by examination of the redox potentials of the two metal ions. Since the peroxy complexes of the models exhibit a structure similar to that of the previously reported fully-oxidized form, the relevance of the model chemistry to the enzyme reaction is discussed.

UR - http://www.scopus.com/inward/record.url?scp=0035119787&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035119787&partnerID=8YFLogxK

U2 - 10.1016/S0162-0134(00)00170-7

DO - 10.1016/S0162-0134(00)00170-7

M3 - Article

C2 - 11293543

AN - SCOPUS:0035119787

VL - 83

SP - 239

EP - 246

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 4

ER -