The isolation and purification of cytochrome c1 from bovine heart

König, B.W.; Schilder, Lisa; Tervoort, M.J.; Gelder, B.F. Van

doi:10.1016/0005-2795(80)90180-4

Cited by 36 publications

(3 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Yu et al (149) developed a purification procedure resulting in a subcomplex of cytochrome c 1 with subunit 8. A preparation reportedly giving a single band was described by Konig et al (150). Kim & King (151,152) later developed improved preparations of one-and two-subunit cytochrome c 1 .…”

Section: Cytochrome C 1 Is a Class I Cytochromementioning

confidence: 99%

Structure and Function of CytochromebcComplexes

Berry

Guergova-Kuras²,

Huang³

et al. 2000

Annu. Rev. Biochem.

473

461

View full text Add to dashboard Cite

Key Words oxidoreductase, respiratory chain, electron transfer, crystallography, membrane protein s Abstract The cytochrome bc complexes represent a phylogenetically diverse group of complexes of electron-transferring membrane proteins, most familiarly represented by the mitochondrial and bacterial bc 1 complexes and the chloroplast and cyanobacterial b 6 f complex. All these complexes couple electron transfer to proton translocation across a closed lipid bilayer membrane, conserving the free energy released by the oxidation-reduction process in the form of an electrochemical proton gradient across the membrane. Recent exciting developments include the application of site-directed mutagenesis to define the role of conserved residues, and the emergence over the past five years of X-ray structures for several mitochondrial complexes, and for two important domains of the b 6 f complex. CONTENTS

show abstract

Section: Cytochrome C 1 Is a Class I Cytochromementioning

confidence: 99%

Structure and Function of CytochromebcComplexes

Berry

Guergova-Kuras²,

Huang³

et al. 2000

Annu. Rev. Biochem.

473

461

View full text Add to dashboard Cite

show abstract

“…The small hinge protein was required for the formation of this complex (4). Recently, electron transfer between cytochromes c1 and c has been reinvestigated by Konig et al (5) using a c1 preparation claimed to contain only one heme peptide (6). They suggested the stable c1-H-c complex as an intermediate in the electron-transfer mechanism (5).…”

mentioning

confidence: 99%

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Kim¹,

Balny²,

King³

1984

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

View full text Add to dashboard Cite

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.

show abstract

“…The sedimentation equilibrium technique shows one-band cytochrome cx to be MT 44000 in 50 mM potassium phosphate buffer, pH 7.4, containing 1% cholate. Kónig et al (1980) have also reported MT 45 000 by the ultracentrifuge technique and 31000 by SDS-PAGE. The higher value is possibly due to the formation of a cytochrome q-cholate complex and probably also a ¿[-phosphate-detergent complex since phosphate binds with cytochrome c [see Taborsky & McCollum (1979) and footnote and references cited therein].…”

Section: Discussionmentioning

confidence: 94%

Preparation and properties of cardiac cytochrome c1

Kim¹,

King²

1987

Biochemistry

View full text Add to dashboard Cite

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.

show abstract

The isolation and purification of cytochrome c1 from bovine heart

Cited by 36 publications

References 23 publications

Structure and Function of CytochromebcComplexes

Structure and Function of CytochromebcComplexes

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Preparation and properties of cardiac cytochrome c1

Contact Info

Product

Resources

About