Studies of the heme components of cytochrome c oxidase by EPR spectroscopy

Gelder, B.F. Van; Beinert, Helmut

doi:10.1016/0005-2728(69)90219-9

Cited by 281 publications

(107 citation statements)

References 28 publications

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“…This structural determination explained the slow reactivity with inhibitors [ 11 ]. The structure also affords the anti-ferromagnetic coupling in the active site that was postulated [12] on the basis of EPR signals.…”

Section: Introductionmentioning

confidence: 62%

Structural features of the copper‐depleted cytochrome oxidase from beef heart: iron exafs

Powers¹,

Chance

Ching³

et al. 1982

FEBS Letters

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Section: Introductionmentioning

confidence: 62%

Structural features of the copper‐depleted cytochrome oxidase from beef heart: iron exafs

Powers¹,

Chance

Ching³

et al. 1982

FEBS Letters

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“…CuEDTA (0.1 mM) in 20% glycerol was used as a primary standard for both the low-spin heme signals and the copper signal of the oxidase. In the latter an arbitrary baseline was assumed (34).…”

Section: Resultsmentioning

confidence: 99%

“…Thus beef heart cytochrome oxidase reveals only one low-spin heme a and one copper (27,34) in the EPR experiment and the other heme a and copper are thought to reside in close physical proximity with a high-spin form of Fe3+ antiferromagnetically coupled to Cu2+ (37)(38)(39)(40). Only one of the a hemes can bind CO (41).…”

Section: Discussionmentioning

confidence: 99%

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

Fee¹,

Choc²,

Findling³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

102

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“…The untreated sample showed also a relatively narrow peak at g ϭ 3.00 arising from the low spin heme B of the cytochrome ba 3 oxidase, as similarly found in mitochondrial or bacterial terminal oxidases (35)(36)(37)(38). The g ϭ 2.92 shoulder is due to the previously characterized membrane cytochrome c 555 (39).…”

Section: Spectroscopic Analysismentioning

confidence: 55%

New Functional Sulfide Oxidase-Oxygen Reductase Supercomplex in the Membrane of the Hyperthermophilic Bacterium Aquifex aeolicus

Prunetti

Infossi

Brugna

et al. 2010

Journal of Biological Chemistry

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Aquifex aeolicus, a hyperthermophilic and microaerophilic bacterium, obtains energy for growth from inorganic compounds alone. It was previously proposed that one of the respiratory pathways in this organism consists of the electron transfer from hydrogen sulfide (H 2 S) to molecular oxygen. H 2 S is oxidized by the sulfide quinone reductase, a membrane-bound flavoenzyme, which reduces the quinone pool. We have purified and characterized a novel membrane-bound multienzyme supercomplex that brings together all the molecular components involved in this bioenergetic chain. Our results indicate that this purified structure consists of one dimeric bc 1 complex (complex III), one cytochrome c oxidase (complex IV), and one or two sulfide quinone reductases as well as traces of the monoheme cytochrome c 555 and quinone molecules. In addition, this work strongly suggests that the cytochrome c oxidase in the supercomplex is a ba 3 -type enzyme. The supercomplex has a molecular mass of about 350 kDa and is enzymatically functional, reducing O 2 in the presence of the electron donor, H 2 S. This is the first demonstration of the existence of such a respirasome carrying a sulfide oxidase-oxygen reductase activity. Moreover, the kinetic properties of the sulfide quinone reductase change slightly when integrated in the supercomplex, compared with the free enzyme. We previously purified a complete respirasome involved in hydrogen oxidation and sulfur reduction from Aquifex aeolicus. Thus, two different bioenergetic pathways (sulfur reduction and sulfur oxidation) are organized in this bacterium as supramolecular structures in the membrane. A model for the energetic sulfur metabolism of Aquifex aeolicus is proposed.

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Studies of the heme components of cytochrome c oxidase by EPR spectroscopy

Cited by 281 publications

References 28 publications

Structural features of the copper‐depleted cytochrome oxidase from beef heart: iron exafs

Structural features of the copper‐depleted cytochrome oxidase from beef heart: iron exafs

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

New Functional Sulfide Oxidase-Oxygen Reductase Supercomplex in the Membrane of the Hyperthermophilic Bacterium Aquifex aeolicus

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