Results 11 to 20 of about 373,942 (257)

Crystallographic studies of cytochrome c and cytochrome c oxidase [PDF]

open access: yesThe Journal of Biochemistry, 2021
I started on crystallographic studies of cytochrome c (Cyt.c) in the later 1960s at Institute for Protein Research, Osaka University. The institute successfully built the structural model of ferro-Cyt.c by the multiple heavy atom replacement method in the early 1970s.
openaire   +2 more sources

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c

open access: yesmBio, 2023
Heme, an essential molecule for virtually all living organisms, acts primarily as a cofactor in a large number of proteins. However, how heme is mobilized from the site of synthesis to the locations where hemoproteins are assembled remains largely ...
Sirui Han   +4 more
doaj   +1 more source

Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c

open access: yesRedox Biology, 2018
In this work, we measured the effect of cytochrome c on the NADH-dependent superoxide anion production by synaptic plasma membrane vesicles from rat brain.
Alejandro K. Samhan-Arias   +5 more
doaj   +1 more source

The effect of cardiolipin side chain composition on cytochrome c protein conformation and peroxidase activity

open access: yesPhysiological Reports, 2021
Skeletal muscle, a highly active tissue, makes up 40% of the total body weight. This tissue relies on mitochondria for ATP production, calcium homeostasis, and programed cell death.
Jennifer A. Wilkinson   +2 more
doaj   +1 more source

Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c

open access: yesBiosensors, 2023
Cytochrome c (Cytc) is a key redox protein for energy metabolism and apoptosis in cells. The activation of Cytc is composed of several steps, including its transfer to the mitochondrial membrane, binding to cytochrome c heme lyase (CCHL) and covalent ...
Mehmet Yunus Genceroglu   +3 more
doaj   +1 more source

Cytochrome c and superoxide [PDF]

open access: yesJBIC Journal of Biological Inorganic Chemistry, 2013
Wegerich et al. (J. Biol. Inorg. Chem. 18:429-440, 2013), working with singly modified human cytochromes c, claim to have found a new mechanism for the reduction of iron(III) cytochrome c by superoxide. I show that electron transfer by way of the solvent-accessible haem edge - a mechanism not considered by Wegerich et al.
openaire   +4 more sources

Mitochondrial DNA variation in the endangered fish Dawkinsia tambraparniei (Actinopterygii: Cypriniformes: Cyprinidae) from southern Western Ghats, India [PDF]

open access: yesActa Ichthyologica et Piscatoria, 2014
Background. Dawkinsia tambraparniei (Silas, 1954) is confined to an area not exceeding 100 km2 within a single watershed—the Tamiraparani River, southern Western Ghats, India.
K. Kannan   +3 more
doaj   +3 more sources

Structure-Function Analysis of the Bifunctional CcsBA Heme Exporter and Cytochrome c Synthetase

open access: yesmBio, 2018
Although intracellular heme trafficking must occur for heme protein assembly, only a few heme transporters have been unequivocally discovered and nothing is known about their structure or mechanisms.
Molly C. Sutherland   +5 more
doaj   +1 more source

Import of cytochrome c into mitochondria. Cytochrome c heme lyase [PDF]

open access: yesEuropean Journal of Biochemistry, 1987
The import of cytochrome c into mitochondria can be resolved into a number of discrete steps. Here we report on the covalent attachment of heme to apocytochrome c by the enzyme cytochrome c heme lyase in mitochondria from Neurospora crassa. A new method was developed to measure directly the linkage of heme to apocytochrome c. This method is independent
D W, Nicholson, H, Köhler, W, Neupert
openaire   +2 more sources

Damage to proteins by peroxidized lipids

open access: yesJournal of Lipid Research, 1963
The purpose of this research was to determine the mechanism of damage to protein by the free radical intermediates formed during the peroxidation of lipids. The reaction system consisted of linolenic acid, cytochrome c, and oxygen.
I.D. Desai, A.L. Tappel
doaj   +1 more source

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