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 +4 more
openaire +2 more sources
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.
Carsten Sanders +2 more
openaire +3 more sources
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 ...
Mark A. Smith +9 more
openaire +2 more sources
Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals [PDF]
, 2004 Defects in heme biosynthesis have been associated with a large number of diseases, but mostly recognized in porphyrias, which are neurovisceral or cutaneous disorders caused by the accumulation of biosynthetic intermediates.
Barrientos, Antoni +2 more
core +1 more source
Transport of proteins across mitochondrial membranes [PDF]
, 1994 The vast majority of proteins comprising the mitochondrion are encoded by nuclear genes, synthesized on ribosomes in the cytosol, and translocated into the various mitochondrial subcompartments. During this process proteins must cross the lipid membranes
Neupert, Walter
core +1 more source
Biogenesis of Cytochrome c in Neurospora crassa [PDF]
, 1978 # 1. Precipitating antibodies specific for apocytochrome c and holocytochrome c, respectively, were employed to study synthesis and intracellular transport of cytochrome c in Neurospora in vitro. # 2.
Korb, Harald, Neupert, Walter
core +1 more source
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).
T Yonetani, H Anni
openaire +2 more sources
Taxonomy of the Crematogaster degeeri-species-assemblage in the Malagasy region (Hymenoptera: Formicidae) [PDF]
, 2013 We revise the species-level taxonomy of the Crematogaster (Crematogaster) degeerispecies-assemblage, a group of related ants occuring in Madagascar and the wider Malagasy region, and further provide an identification key to all species-groups of the ...
Blaimer, Bonnie B., Fisher, Brian L.
core +3 more sources
Tissue-specific and species-specific distribution of -SH groups in cytochrome c oxidase subunits [PDF]
European Journal of Biochemistry, 1986 Cytochrome c oxidase was isolated from pig, bovine, rat and human tissues including liver, heart, diaphragm and kidney. The native and the sodium-dodecyl-sulfate (SDS)-dissociated enzymes were labelled under optimal conditions with N-ethyl-[2,3-14C]maleimide before and after reduction with dithiothreitol, separated into 13 subunits by SDS gel ...
Bernhard Kadenbach, Annemarie Stroh
openaire +3 more sources
Probing a Complex of Cytochromecand Cardiolipin by Magnetic Circular Dichroism Spectroscopy: Implications for the Initial Events in Apoptosis [PDF]
, 2011 Oxidation of cardiolipin (CL) by its complex with cytochrome c (cyt c) plays a crucial role in triggering apoptosis. Through a combination of magnetic circular dichroism spectroscopy and potentiometric titrations, we show that both the ferric and ferrous
Armstrong F. A. +42 more
core +1 more source