The cytochrome complement of Haemophilus parasuis

1984 ◽  
Vol 30 (6) ◽  
pp. 763-773 ◽  
Author(s):  
D. F. Niven
Keyword(s):  
Growth Rate ◽  
Cytochrome C ◽  
Osmotic Shock ◽  
Shock Treatment ◽  
Redox Properties ◽  
Haemophilus Parasuis ◽  
Bacterial Concentration ◽  
Cytochromes C ◽  
Membrane Bound ◽  
Cytochrome Content

Spectral analyses with subcellular fractions derived from Haemophilus parasuis demonstrated that this organism could synthesize membrane-bound and soluble CO- and NO-binding c-type cytochromes in addition to the membrane-bound cytochromes d, a1, b, and c; cytochromes d, a1, and o were identified as potential oxidases. The membrane-bound and soluble CO- and NO-binding cytochromes c were not spectrally variant cytochromes c, and the redox properties of the soluble cytochrome (reducible by NADH but not by succinate or ascorbate plus N,N,N′,N′-tetramethyl-p-phenylenediamine) suggested that it, at least, was a low-potential cytochrome; up to 68% of the soluble cytochrome c could be released from the organisms by osmotic-shock treatment, demonstrating its extracytoplasmic location. The cytochrome content of H. parasuis was influenced by both the composition of the growth medium and the phase of growth; it is suggested that the bacterial concentration and growth rate, and therefore the availability of oxygen, regulated cytochrome synthesis.

Cytochromes and Anaerobic Sulfide Oxidation in the Purple Sulfur Bacterium Chromatium warmingii

1983 ◽  
Vol 38 (11-12) ◽  
pp. 960-967 ◽  
Author(s):  
Ursula Wermter ◽  
Ulrich Fischer
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Elemental Sulfur ◽  
Sulfide Oxidation ◽  
Sodium Dodecylsulfate ◽  
Gel Filtration ◽  
Purple Sulfur Bacterium ◽  
Cytochromes C ◽  
Membrane Bound ◽  
Reduced State

Two soluble acidic c-type cytochromes - c' and c-552 - were isolated by ion exchange :hromatography, gel filtration and ammonium sulfate fractionation. Cytochrome c' is a high-spir tochrome with maxima at 399 nm. 490 nm. and 634 nm in the oxidized form and at 550 nm. 15 nm and a characteristic shoulder at 434 nm in the reduced state. The best purity index obtained A280/A399) was 0.35. Cytochrome c' is autoxidizable, has a molecular weight of 12 000 (estimate by sodium dodecylsulfate electrophoresis), a midpoint redoxpotential of + 10 mV and an iso­electric point at pH 4.0. The reduced cytochrome c' reacts with carbon monoxide. The reaction reversible. Cytochrome c-552 shows maxima at 552 nm, 523 nm and 417 nm in the reduced for ind at 408 nm in the oxidized state. The best purity index obtained (A280/A408) was 0.94. "ytochrome c-552 has a molecular weight of 30 000 and an isoelectric point between pH 4.1 Zhromatium warmingii also contains a membrane-bound cytochrome c-552. During anaerobic sulfide oxidation, elemental sulfur and sulfate were formed at the same time. When all sulfide consumed by the cells, the remaining intracellular elemental sulfur was further oxidized to sulfate

scholarly journals The electron-transport chains of the obligate methylotroph Methylophilus methylotrophus

1980 ◽  
Vol 192 (2) ◽  
pp. 429-439 ◽  
Author(s):  
Andrew R. Cross ◽  
Christopher Anthony
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Redox Potentials ◽  
Obligate Methylotroph ◽  
Methylophilus Methylotrophus ◽  
Cytochrome O ◽  
Cytochromes C ◽  
Band Absorption ◽  
Membrane Bound ◽  
Α Band

The cytochrome complement of Methylophilus methylotrophus and its respiratory properties were determined during batch culture and in continuous culture under conditions of methanol-, nitrogen- and O2-limitation. About 35% of the cytochrome c produced by the bacteria was released into the growth medium, and of the remaining cytochrome c about half was membrane-bound and half was soluble. Two cytochromes c were always present on membranes (redox potentials 375mV and 310mV), and these probably correspond to the soluble cytochromes c described previously [Cross & Anthony (1980) Biochem. J.192, 421–427]. A third minor component of cytochrome c (midpoint potential 356mV) was only detected on membranes of methanol-limited bacteria. M. methylotrophus always contained two membrane-bound cytochromes b with α-band absorption maxima of about 556 and 563nm (measured at room temperature) and midpoint potentials of 110 and 60mV respectively. There appeared to be relatively more of the cytochrome b563 in methanol-limited bacteria. A third b-type cytochrome with an α-band absorption maximum at 558 (at 77K) reacted with CO and had a high midpoint redox potential (260mV); it is thus a potential oxidase and hence is called cytochrome o. The roles of these cytochromes in electron transport were confirmed by investigating the patterns of respiratory inhibition. It is proposed that two cytochromes are physiological oxidases: cytochrome a+a3, which is present only in methanol-limited conditions, and the cytochrome o, which is induced 10-fold in conditions of methanol excess. Schemes for electron transport from methanol and NAD(P)H to O2 in M. methylotrophus under various limitations are proposed. Spectra and potentiometric titrations of cytochromes in whole cells and membranes of M. methylotrophus grown under various nutrient limitations have been deposited as Supplementary Publication SUP 50111 (10 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

scholarly journals Comparison of yeast and beef cytochrome c oxidases. Kinetics and binding of horse, fungal, and Euglena cytochromes c.

1979 ◽  
Vol 254 (23) ◽  
pp. 11973-11981 ◽  
Author(s):  
J.K. Dethmers ◽  
S. Ferguson-Miller ◽  
E. Margoliash
Keyword(s):  
Cytochrome C ◽  
Cytochromes C

scholarly journals Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c.

1977 ◽  
Vol 252 (2) ◽  
pp. 574-582 ◽  
Author(s):  
D L Brautigan ◽  
B A Feinberg ◽  
B M Hoffman ◽  
E Margoliash ◽  
J Preisach ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Epr Spectra ◽  
Cytochromes C

scholarly journals The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

1973 ◽  
Vol 131 (3) ◽  
pp. 485-498 ◽  
Author(s):  
R. P. Ambler ◽  
Margaret Wynn
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Mitochondrial Cytochrome ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system

1982 ◽  
Vol 60 (6) ◽  
pp. 613-623 ◽  
Author(s):  
P. Nicholls ◽  
J.-K. Kim
Keyword(s):  
Cytochrome C ◽  
Oxygen Uptake ◽  
Cytochrome C Oxidase ◽  
Submitochondrial Particles ◽  
Inhibitory Interaction ◽  
Cytochromes C ◽  
Subsequent Step ◽  
Oxidase Enzyme ◽  
Rapid Reaction ◽  
The One

Anomalies both kinetic and equilibrium in nature are described for the inhibition of cytochrome c oxidase activity by sulphide in the isolated enzyme and in submitochondrial particles. These anomalies are related to the involvement of more than 1 mol of sulphide in the blockage of one cytochrome aa3 centre. Sulphide reduces resting cytochrome a3, a reaction that results in oxygen uptake and the loss of a sulphide molecule. Sulphide can also reduce cytochromes c and a; in the former case, a part of the one-equivalent oxidation product, presumed to be the SH∙ radical, reacts with oxygen. Such oxygen uptake is also seen under aerobic conditions when ferricyanide reacts with sulphide. Three phases are identified in the inhibitory interaction of sulphide with the cytochrome c oxidase enzyme itself: an initial rapid reaction involving sulphide oxidation, oxygen uptake, and conversion of cytochrome aa3 into the low-spin "oxyferri" form; a subsequent step in which sulphide reduces cytochrome a; and the final inhibitory step in which a third molecule of sulphide binds the a3 iron centre in the cytochrome [Formula: see text] (oxy) species to give cytochrome [Formula: see text]. The initial events parallel some of the events in the interaction of the cytochrome c – cytochrome aa3 system with monothiols; the final inhibitory event resembles that with cyanide.

scholarly journals Structure of the copper sites in membrane-bound cytochrome c oxidase.

1987 ◽  
Vol 262 (7) ◽  
pp. 3160-3164
Author(s):  
L. Powers ◽  
B. Chance ◽  
Y.C. Ching ◽  
C.P. Lee
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Membrane Bound ◽  
Copper Sites

Cytochrome c, A Membrane-Bound Enzyme

1976 ◽  
pp. 43-86 ◽  
Author(s):  
Jane Vanderkooi ◽  
Maria Erecińska
Keyword(s):  
Cytochrome C ◽  
Membrane Bound
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