Results 1 to 10 of about 242,283 (275)

Yeast cytochrome c peroxidase. Coordination and spin states of heme prosthetic group. [PDF]

Journal of Biological Chemistry, 1987
Electronic absorption and electron paramagnetic resonance (EPR) spectroscopic examinations revealed that a freshly prepared cytochrome c peroxidase (CCP) contains a penta-coordinated high spin ferric protoheme group. The penta-coordinated high spin state of fresh CCP is maintained in a remarkably wide range of pH (4-8).
Takashi Yonetani, Helen Anni
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Is cytochrome c oxidase subunit I (COI) the right DNA barcoding marker for the Chaetopteryx villosa group? [PDF]

ARPHA Conference Abstracts, 2021
Chaetopteryx villosa (Fabricius, 1798) is a caddisfly species distributed throughout Europe, except in the Balkan and Apennine Peninsula. However, phylogenetically close species belonging to the C. villosa group are widespread throughout entire Europe. Species of this group (C. villosa, C. gessneri, C. fusca, C. sahlbergi, C. atlantica, C. bosniaca, C.
Dalila Destanović, Lejla Ušanović, Lejla Lasić, Jasna Hanjalić, Belma Kalamujić Stroil   +4 more
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Structure of an electron transfer complex. II. Chemical modification of carboxyl groups of cytochrome c peroxidase in presence and absence of cytochrome c.

Journal of Biological Chemistry, 1985
Cytochrome c peroxidase forms an electron transfer complex with cytochrome c. The complex is governed by ionic bonds between side chain amino groups of cytochrome c and carboxyl groups of peroxidase. To localize the binding site for cytochrome c on the peroxidase, we have used the method of differential chemical modification.
Rolf Bechtold, Hans Rudolf Bosshard
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Assignment of the CO-sensitive carboxyl group in mitochondrial forms of cytochrome c oxidase using yeast mutants [PDF]

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2012
Point mutations of E243D and I67N were introduced into subunit I of a 6histidine-tagged (6H-WT) form of yeast Saccharomyces cerevisiae mitochondrial cytochrome c oxidase. The two mutants (6H-E243D(I) and 6H-I67N(I)) were purified and showed ≈50 and 10% of the 6H-WT turnover number. Light-induced CO photolysis FTIR difference spectra of the 6H-WT showed
Amandine Maréchal, Brigitte Meunier, Peter R. Rich   +2 more
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Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c‐type cytochromes [PDF]

Molecular Microbiology, 2006
SummaryIn all organisms, haem is post‐translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c‐type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem–apocytochrome ligation per se.
Serdar Turkarslan, Carsten Sanders, Fevzi Daldal   +2 more
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Vibrational structure of the formyl group on heme a. Implications on the properties of cytochrome c oxidase

Biophysical Journal, 1991
Resonance Raman spectra have been recorded for heme a derivatives in which the oxygen atom of the formyl group has been isotopically labeled and for Schiff base derivatives of heme a in which the Schiff base nitrogen has been isotopically labeled. The 14N-15N isotope shift in the C = N stretching mode of the Schiff base is close to the theoretically ...
Sae‐Won Han, Yern Chee Ching, Sharon Hammes‐Schiffer, Denis L. Rousseau   +3 more
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Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groups [PDF]

Current Issues in Molecular Biology
Neuroglobin (Ngb) is a cytosolic heme protein that plays an important role in protecting cells from apoptosis through interaction with oxidized cytochrome c (Cyt c) released from mitochondria. The interaction of reduced Ngb and oxidized Cyt c is accompanied by electron transfer between them and the reduction in Cyt c.
Marina A. Semenova, Zhanna V. Bochkova, Olga Mikhailovna Smirnova, Г. В. Максимов, М. П. Кирпичников, Д. А. Долгих, Nadezda A. Brazhe, Rita V. Chertkova   +7 more
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Suitability of Adenosine Derivatives in Improving the Activity and Stability of Cytochrome c under Stress: Insights into the Effect of Phosphate Groups [PDF]

The Journal of Physical Chemistry B, 2023
It is well known that adenosine and its phosphate derivatives play a crucial role in biological phenomena such as apoptosis and cell signaling and act as the energy currency of the cell. Although their interactions with various proteins and enzymes have been described, the focus of this work is to demonstrate the effect of the phosphate group on the ...
Pranav Bharadwaj, Sachin M. Shet, Meena Bisht, Dheeraj Kumar Sarkar, Gregory Franklin, S.K. Nataraj, Dibyendu Mondal   +6 more
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Heme-a, the heme prosthetic group of cytochrome c oxidase, is increased in Alzheimer's disease [PDF]

Neuroscience Letters, 2009
Heme-a, is the heme prosthetic group of cytochrome c oxidase (COX), the terminal complex of the mitochondrial electron transport chain. We measured heme-a levels in postmortem brain tissue from nine patients diagnosed with dementia: Alzheimer's disease (AD) was the primary diagnosis in five, AD/diffuse Lewy body disease (DLBD) was diagnosed in two ...
Barney E. Dwyer, Meghan L. Stone, Nadia Gorman, Peter R. Sinclair, George Perry, Mark A. Smith, Xiongwei Zhu   +6 more
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Thermodynamic Data for Myoglobin, Hæmoglobin and Cytochrome-c Reactions, and the Position of the Hæm Groups [PDF]

Nature, 1955
CONANT1 first put forward the idea that the haems in haemoglobin are held by two bonds of unequal strength between the iron and groups in the protein on both sides of the haem disk, the weaker bond breaking when combination with oxygen, carbon monoxide, etc., occurs.
Philip George, G. I. H. Hanania
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