Components of cytochrome c oxidase detectable by EPR spectroscopy

Hartzell, Charles R.; Beinert, Helmut

doi:10.1016/0005-2728(74)90178-9

Cited by 245 publications

(149 citation statements)

References 23 publications

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“…This was demonstrated previously in an extensive study of cyanide-binding kinetics, optical spectra and EPR spectra of several preparations commonly used [4]. By modifying the method of Hartzell and Beinert [25], these authors could demonstrate that a carefully handled enzyme has monophasic cyanide-binding kinetics and that the Soret maximum of the oxidized enzyme is not blue-shifted beyond 420 nm. Following the criteria of this work, our preparation appears not to be altered by the purification procedure.…”

Section: Discussionmentioning

confidence: 60%

Purification of cytochrome‐c oxidase retaining its pulsed form

Brandt

Schägger

Jagow

1989

European Journal of Biochemistry

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A new purification procedure for cytochrome‐c oxidase from bovine heart mitochondria is described. The enzyme was purified by selective solubilization in Triton X‐100 and subsequent hydroxyapatite and gel chromatography. The preparation was highly pure and active. The subunit composition and steady‐state kinetics were found to be the same as thoes reported for other preparations. In contrast to most of the previously published protocols the method presented here resulted in a preparation which had a rapid intramolecular electron transfer from cytochrome a to cytochrome a3, i.e. it was found to have retained its pulsed state. This correlated with monoexponential cyanide‐binding kinetics. The formation of resting kinetics biphasic cyanide‐binding kinetics was shown to be induced by a short incubation at pH 5.0.

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Section: Discussionmentioning

confidence: 60%

Purification of cytochrome‐c oxidase retaining its pulsed form

Brandt

Schägger

Jagow

1989

European Journal of Biochemistry

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“…The gel composition was 7% acrylamide with 1 part in 10 of bisacrylamide in gels a-h and 8% and 1:15 in gels i-k. The molecular weight standards (gels b, d, f, h, k) were obtained as BioRad low molecular weight kit: phosphorylase b (94,000), bovine serum albumin (68,000), ovalbumin (43,000), carbonic anhydrase (30,000), soybean trypsin inhibitor (21,000), and lysozyme (14,300 (20).1 Also shown in Fig. 2, gel oxidase activity.J The acid/acetone extract of the bacterial cytochrome complex was subjected to heme analysis by forming the pyridine hemochromogen and was found to contain only heme a.…”

Section: Resultsmentioning

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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“…Furthermore, although both copper ions are believed to be cupric in the fully oxidised state, only one can be detected in the e.p.r. experiments [3].…”

Section: Introductionmentioning

confidence: 95%

“…as the low spin ferric form. A minor component, about 2.3% of the total heme, is detectable as the typical g = 6 high spin ferric signal [3]. Furthermore, although both copper ions are believed to be cupric in the fully oxidised state, only one can be detected in the e.p.r.…”

Section: Introductionmentioning

confidence: 98%