The reaction between cytochrome C1 and cytochrome C

König, B.W.; Wilms, J.; Gelder, B.F. Van

doi:10.1016/0005-2728(81)90069-4

Cited by 33 publications

(17 citation statements)

References 25 publications

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“…These results are quite different from those reported (5) 1 1 glutamic acid residues are linked consecutively (7). There is no spectral absorption at >300 nm, and even the absorption coefficient at the 280-nm region is very low because there is no tyrosine or tryptophan, but only two each of disulfide linkages and phenylalanine residues (8).…”

Section: J)contrasting

confidence: 56%

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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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Section: J)contrasting

confidence: 56%

“…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).…”

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confidence: 99%

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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“…Stopped-flow spectroscopy has been used to measure electron transfer between Cc and cyt c 1 at high ionic strength, where a second-order reaction between the two molecules in solution is observed (5,6,39). However, the reaction becomes too fast to resolve by stopped-flow spectroscopy as the ionic strength is decreased below 200 mM.…”

Section: Design Of Ru Z -39-cc For Rapid Electron Transfer Betweenmentioning

confidence: 99%

Design of a Ruthenium-Labeled Cytochrome c Derivative to Study Electron Transfer with the Cytochrome bc₁ Complex

et al. 2003

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A new ruthenium-cytochrome c derivative was designed to study electron transfer from cytochrome bc1 to cytochrome c (Cc). The single sulfhydryl on yeast H39C;C102T iso-1-Cc was labeled with Ru(2,2'-bipyrazine)2(4-bromomethyl-4'-methyl-2,2'-bipyridine) to form Ru(z)-39-Cc. The Ru(z)-39-Cc derivative has the same steady-state activity with yeast cytochrome bc1 as wild-type yeast iso-1-Cc, indicating that the ruthenium complex does not interfere in the binding interaction. Laser excitation of reduced Ru(z)-39-Cc results in electron transfer from heme c to the excited state of ruthenium with a rate constant of 1.5 x 10(6) x s(-1). The resulting Ru(I) is rapidly oxidized by atmospheric oxygen in the buffer. The yield of photooxidized heme c is 20% in a single flash. Flash photolysis of a 1:1 complex between reduced yeast cytochrome bc1 and Ru(z)-39-Cc at low ionic strength leads to rapid photooxidation of heme c, followed by intracomplex electron transfer from cytochrome c1 to heme c with a rate constant of 1.4 x 10(4) x s(-1). As the ionic strength is raised above 100 mM, the intracomplex phase disappears, and a new phase appears due to the bimolecular reaction between solution Ru-39-Cc and cytochrome bc1. The interaction of yeast Ru-39-Cc with yeast cytochrome bc1 is stronger than that of horse Ru-39-Cc with bovine cytochrome bc1, suggesting that nonpolar interactions are stronger in the yeast system.

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“…In a number of studies, horse heart cytochrome c (cyt c), a well-characterized respiratory electrontransport protein, has been used as a probe for investigation of the biological functions of other electron-transport proteins. [3][4][5][6][7][8][9][10][11][12][13][14] Cyt c accepts electrons from cytochrome c reductase and donates electrons to cytochrome c peroxidase and cytochrome c oxidase at the end of the respiratory electrontransport chain.[3] Investigations with various lysine-modified versions of cyt c have concluded that the intermolecular electron-transfer reactions are facilitated by interaction of the positively charged cyt c with the negatively charged surfaces of its redox partners. [4][5][6][7][8][9] The intermolecular van der Waals, hydrogen bonding, and electrostatic interactions involved in the formation of the associated complexes of cyt c with cytochrome c reductase or with cytochrome c peroxidase have been characterized from crystal structures of these complexes.…”

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confidence: 99%

“…[3][4][5][6][7][8][9][10][11][12][13][14] Cyt c accepts electrons from cytochrome c reductase and donates electrons to cytochrome c peroxidase and cytochrome c oxidase at the end of the respiratory electrontransport chain.…”

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confidence: 99%

Electron‐Transfer Reactions through the Associated Interaction between Cytochrome c and Self‐Assembled Monolayers of Optically Active Cobalt(III) Complexes: Molecular Recognition Ability Induced by the Chirality of the Cobalt(III) Units

Takahashi¹,

Inomata²,

Funahashi³

et al. 2007

Chemistry A European J

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Self-assembled monolayers (SAMs) of optically active Co(III) complexes ((S)-2/(R)-2) that contain (S)- or (R)-phenylalanine derivatives as a molecular recognition site were constructed on Au electrodes ((S)-2-Au/(R)-2-Au). Molecular recognition characteristics induced by the S and R configurations were investigated by measurements of electron-transfer reactions with horse heart cytochrome c (cyt c). The electrochemical studies indicate that the maximum current of cyt c reduction is obtained when the Au electrode is modified by 2 with a moderate coverage of approximately 4.0 x 10(-11) mol cm(-2). Since the Au electrode is not densely packed with the Co(III) units at this concentration, we conclude that the penetrative association process between cyt c and the Co(III) unit plays an important role in this electron-transfer system. The differences in the electron-transfer rates of (S)-2-Au and (R)-2-Au increase with increasing scan rates, a result indicating that the chiral ligand has an influence on the rate of association of the complexes with cyt c. 3-Au has a mixed monolayer composed of 2 and hexanethiol and exhibits electron-transfer behavior comparable to 2-Au. The difference in the association rates of (S)-3-Au and (R)-3-Au is larger than that between (S)-2-Au and (R)-2-Au, which indicates that the molecular recognition ability of 3-Au has been enhanced by filling the gap between molecules of 2 with hexanethiols. The differences in the oxidation rates of cyt c(II) between (S)-2-Au and (R)-2-Au and between (S)-3-Au and (R)-3-Au were larger than the differences in the rates of the reduction of cyt c(III); this suggests that the size of the heme crevice varies according to the oxidation state of cyt c.

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The reaction between cytochrome C1 and cytochrome C

Cited by 33 publications

References 25 publications

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Design of a Ruthenium-Labeled Cytochrome c Derivative to Study Electron Transfer with the Cytochrome bc₁ Complex

Electron‐Transfer Reactions through the Associated Interaction between Cytochrome c and Self‐Assembled Monolayers of Optically Active Cobalt(III) Complexes: Molecular Recognition Ability Induced by the Chirality of the Cobalt(III) Units

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The reaction between cytochrome C1 and cytochrome C

Cited by 33 publications

References 25 publications

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Kinetics of electron transfer between cardiac cytochromes c1 and c.

Design of a Ruthenium-Labeled Cytochrome c Derivative to Study Electron Transfer with the Cytochrome bc1 Complex

Electron‐Transfer Reactions through the Associated Interaction between Cytochrome c and Self‐Assembled Monolayers of Optically Active Cobalt(III) Complexes: Molecular Recognition Ability Induced by the Chirality of the Cobalt(III) Units

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Design of a Ruthenium-Labeled Cytochrome c Derivative to Study Electron Transfer with the Cytochrome bc₁ Complex