Cardiac Cytochrome
            <i>c</i>
            <sub>1</sub>

King, Tsoo E.

doi:10.1002/9780470122990.ch5

Advances in Enzymology - And Related Areas of Molecular Biology

1983

DOI: 10.1002/9780470122990.ch5

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Cardiac Cytochrome c ₁

Tsoo E. King

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1984

1987

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Cited by 4 publications

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The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

Loon¹,

Groot²,

Haan³

et al. 1984

The EMBO Journal

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We have determined the DNA sequence of the nuclear gene coding for the 17‐kd subunit VI of the ubiquinol‐cytochrome c reductase. The reading frame found encodes a putative polypeptide of 17 394 daltons. This protein is highly unusual: 38% of its residues are acidic and 14% are basic amino acids. The most notable feature in the protein sequence is a stretch of 25 consecutive acidic amino acids. The polypeptide has homology with the 9‐kd so‐called ‘hinge’ protein of beef‐heart complex III, which also has a cluster of acidic residues. Acidic amino acids are likely to be essential for the function of these proteins, since their degree of conservation is higher than that of other residues.

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The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

Loon¹,

Groot²,

Haan³

et al. 1984

The EMBO Journal

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Preparation and properties of cardiac cytochrome c1

Kim¹,

King²

1987

Biochemistry

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A method for the large-scale isolation of beef heart mitochondrial cytochrome c1 in high purity was developed. This method gave higher yield of "one-band" cytochrome c1 than previously reported [Kim, C. H., & King, T. E. (1981) Biochem. Biophys. Res. Commun. 102, 607-614]. In addition, the present method was effective in the preparation of "two-band" cytochrome c1 which was used to prepare the hinge protein according to the principle of sequential resolution [Kim, C. H., & King, T. E. (1983) J. Biol. Chem. 258, 13543-13551]. The isolation of one-band and two-band cytochrome c1 by this procedure could be completed within 3 or 4 days starting with succinate-cytochrome c reductase. One-band cytochrome c1 showed a molecular weight of 44,000 by sedimentation equilibrium and 29,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The disparities in these data from the actual value of 27,924 by amino acid sequence analysis, as previously reported [Wakabayashi, S., Matsubara, H., Kim, C. H., & King, T. E. (1982) J. Biol. Chem. 257, 9335-9344], are most probably due to the formation of detergent or detergent-phosphate complex. A comparison of some properties of one-band cytochrome c1 with those of two-band cytochrome c1 clearly showed significant differences between the two preparations. These results suggest the hypothesis that one of the possible roles of the hinge protein in the mitochondrial respiratory chain is to stabilize the conformation of cytochrome c1.

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Kinetics of electron transfer between cardiac cytochromes c1 and c.

Kim¹,

Balny²,

King³

1984

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

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Highly purified cytochrome cl, which consists of only one heme peptide and does not form a stable cl-c complex (cl-H-c complex), was used in studies of electron transfer between cytochromes cl and c. Results show that a stable and ionic-strength-sensitive cl-c complex (i.e., the cl-H-c complex) in the forms of the various oxidation states is not required, in contrast to the current belief of the participation of the complex in the electron transfer between cytochromes cl and c. A minimum mechanism for electron transfer between these two cytochromes is suggested in accord with the experimental results.The molecular mechanism for electron transfer between cytochrome c1 and cytochrome c remains to be clarified. The kinetics of this reaction were first studied (1) using purified preparations of cl (2) (vol/vol) ethylene glycol, the final concentration of the buffer being 20 mM. The protonic activities (paH) of this buffer were 7.4, 7.5, and 7.6 at 20, 0, and -20°C, respectively (cf. refs. 10 and 11). Fast Kinetics and Rapid-Scanning Measurements. Stoppedflow and rapid-scan measurements were performed using a special stopped-flow mixing device (12), designed and built by INSERM (Montpellier), adapted to a Union Giken (model RA 415 and 401) fast-response spectrophotometer (13,14). The temperature of syringes and mixing chamber of the stopped-flow were maintained at ±0.1°C with a circulating Haake bath model f3-Q. Rapid-scan absorption spectra were measured with a multichannel photodiode (maximum speed, 95 x 103 nm sec-1). The spectra were stored in a memory unit and then analyzed with a digital computer system. The kinetic responses were found to be first order, and the observed rate constants (kobs) were determined from a nonlinear least-squares analysis using a computer fitting program. Single values of rate constants reported are the average of at least five experimental determinations. Kinetic constants have been estimated with an error not exceeding ±20%.Absorption spectra were obtained at 20°C or 2°C using either a Cary 219 or an Aminco DW-2 spectrophotometer equipped with a thermostatted cells holder (15). RESULTS AND DISCUSSIONReactions of c2+ with c3+ were measured during stoppedflow rapid mixing of the two cytochromes in 20 mM sodium cacodylate buffer (pH 7.4) at 20C. A typical tracing of kinetics at 416 nm is shown in Fig. 1A. Fig. 1B (Fig. 2, spectrum A). Another difference spectrum was seen when both cytochromes in the oxidized form were mixed and compared with these two cytoAbbreviation: cl-H-c complex; cytochrome cl-hinge protein-cytochrome c complex. 2026The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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Cardiac Cytochrome c ₁

Cited by 4 publications

References 147 publications

The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

Preparation and properties of cardiac cytochrome c1

Kinetics of electron transfer between cardiac cytochromes c1 and c.

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Product

Resources

About

Cardiac Cytochrome c 1

Cited by 4 publications

References 147 publications

The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids.

Preparation and properties of cardiac cytochrome c1

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Contact Info

Product

Resources

About

Cardiac Cytochrome c ₁