Results 41 to 50 of about 2,499,952 (347)

Different reactivity of carboxylic groups of cytochrome c oxidase polypeptides from pig liver and heart [PDF]

FEBS Letters, 1984
Cytochrome c oxidase isozyme Cytochrome c binding domain 1‐Ethyl‐3‐(3‐dimethylaminopropyl)carbodiimide Tissue specificity
Bernhard Kadenbach, Annemarie Stroh
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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
Maréchal, A, Meunier, B, Rich, PR
openaire   +3 more sources

Apoptosis Occurs in Anterior Talofibular Ligament of Chronic Lateral Ankle Instability: Biochemical Evidence from Bench to Bed

Foot & Ankle Orthopaedics, 2022
Category: Ankle; Basic Sciences/Biologics; Sports Introduction/Purpose: Chronic lateral ankle instability (CLAI) is a common entity that can result in degenerative arthritis if left untreated.
Yoon-Chung Kim MD, Sung Hyun Cho
doaj   +1 more source

Rate variation during molecular evolution: creationism and the cytochrome c molecular clock [PDF]

, 2017
Molecular clocks based upon amino acid sequences in proteins have played a major role in the clarification of evolutionary phylogenies. Creationist criticisms of these methods sometimes rely upon data that might initially seem to be paradoxical.
Hofmann James, R.
core   +1 more source

Effect of pH on the thermostability and redox properties of cytochrome c552 from Wolinella succinogenes

Frontiers in Chemical Biology
Cytochrome c552 from Wolinella succinogenes is one of the few examples of a low reduction potential class I c-type cytochrome with a mixture of high/low spin state populations observed in its visible spectrum.
Vitor H. Mordido, Vitor H. Mordido, Vitor H. Mordido, Marta S. P. Carepo, Marta S. P. Carepo, Cristina M. Cordas, Navendu Paul, Jörg Simon, Isabel Moura, Sofia R. Pauleta, Sofia R. Pauleta   +10 more
doaj   +1 more source

Proton translocation in proteins [PDF]

, 1989
The active transport of protons across the low dielectric barrier imposed by biological membranes is accomplished by a plethora of proteins that span the ca. 40 Å of the phospholipid bilayer.
Chan, Sunney I., Copeland, Robert A.
core   +1 more source

Effect of pre-irradiation with different doses, wavelengths, and application intervals of low-level laser therapy on cytochrome c oxidase activity in intact skeletal muscle of rats

Lasers in Medical Science, 2014
Modulation of cytochrome c oxidase activity has been pointed as a possible key mechanism for low-level laser therapy (LLLT) in unhealthy biological tissues.
G. M. Albuquerque-Pontes, R. Vieira, S. S. Tomazoni, Claudia Caires, V. Nemeth, A. A. Vanin, L. Santos, H. Pinto, R. L. Marcos, J. Bjordal, Paulo de Tarso Camillo de Carvalho, E. C. Leal-Junior   +11 more
semanticscholar   +1 more source

Urinary Cytochrome C and Caspase-3 as Novel Biomarker of Renal Function Impairment in Unilateral Ureteropelvic Junction Obstruction Model of Wistar Rats

Research and Reports in Urology, 2020
Jupiter Sibarani,1 Tjahjodjati Tjahjodjati,1 Nur Atik,2 Dedi Rachmadi,3 Akhmad Mustafa1 1Department of Urology, Faculty of Medicine Universitas Padjadjaran, Hasan Sadikin Hospital Bandung, Bandung, Indonesia; 2Department of Biomedical Sciences, Faculty ...
Sibarani J, Tjahjodjati T, Atik N, Rachmadi D, Mustafa A   +4 more
doaj  

Molecular Basis and Consequences of the Cytochrome c-tRNA Interaction. [PDF]

, 2016
The intrinsic apoptosis pathway occurs through the release of mitochondrial cytochrome c to the cytosol, where it promotes activation of the caspase family of proteases.
Christian, Thomas, Hou, Ya-Ming, Liu, Cuiping, Stonestrom, Aaron J, Takase, Ryuichi, Yang, Xiaolu, Yong, Jeongsik   +6 more
core   +2 more sources

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.
Hans Rudolf Bosshard, R Bechtold
openaire   +3 more sources