Results 81 to 90 of about 19,766,647 (382)
In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases
eLife, 2021 Cytochromes c are ubiquitous heme proteins in mitochondria and bacteria, all possessing a CXXCH (CysXxxXxxCysHis) motif with covalently attached heme. We describe the first in vitro reconstitution of cytochrome c biogenesis using purified mitochondrial ...
Molly C Sutherland +8 more
doaj +1 more source
Semisynthetic cytochrome c. [PDF]
Proceedings of the National Academy of Sciences, 1977 Horse heart cytochrome c can be split with cyanogen bromide into a heme peptide (residues 1-65) and a nonheme peptide (residues 66-104). In a process involving (i) complex formation between the two fragments and (ii) restoration of the severed peptide linkage, a fully active cytochrome c preparation can be re-formed.
Leon E. Barstow +6 more
openaire +3 more sources
FEBS Open Bio, EarlyView.Cleavable N‐terminal Thioredoxin fusion enabled soluble expression and purification of otherwise insoluble SARS‐CoV‐2 Nucleocapsid (N) protein. A four‐step purification strategy yielded highly homogeneous, RNA‐free N protein. Binding assays showed high RNA affinity (Kd ~ 28 nm). The study will facilitate high‐resolution structural studies of N protein,
Shweta Singh, Gagan D. Gupta
wiley +1 more source
Molecular Dissection of Bacterial Nanowires
mBio, 2013 The discovery of bacterial conductive structures, termed nanowires, has intrigued scientists for almost a decade. Nanowires enable bacteria to transfer electrons over micrometer distances to extracellular electron acceptors such as insoluble metal oxides
Thomas Boesen, Lars Peter Nielsen
doaj +1 more source
Structure-Guided Recombination Creates an Artificial Family of Cytochromes P450 [PDF]
, 2006 Creating artificial protein families affords new opportunities to explore the determinants of structure and biological function free from many of the constraints of natural selection.
Arnold, Frances H. +5 more
core +1 more source
Interaction of class III cellobiose dehydrogenase with lytic polysaccharide monooxygenase
FEBS Open Bio, EarlyView.The activity of lytic polysaccharide monooxygenase (LPMO) is supported by its auxiliary enzyme cellobiose dehydrogenase (CDH). The catalytic activity of both enzymes is coupled by electron transfer and a cyclic cascade generating substrates for both enzymes – hydrogen peroxide for LPMO and oxidized and non‐oxidized cellobiose and cello‐oligosaccharide ...
Angela Giorgianni +4 more
wiley +1 more source
European Journal of Biochemistry, 1977 The luminescent properties of metal-free, tin(IV) and zinc(II) cytochromes c have been used to characterize the interaction of cytochrome c with mitochondria and cytochrome oxidase. Diminution in the fluorescence yields of tin and zinc cytochrome c occur
J. Vanderkooi +3 more
semanticscholar +1 more source
Resonance Raman Spectroscopy Reveals that Substrate Structure Selectively Impacts the Heme-Bound Diatomic Ligands of CYP17 [PDF]
, 2013 An important function of steroidogenic cytochromes P450 is the transformation of cholesterol to produce androgens, estrogens, and the corticosteroids.
Gregory, Michael C. +3 more
core +2 more sources
FEBS Open Bio, EarlyView.Caloric restriction that extends lifespan induces the expression of PGC‐1α and MIPEP in white adipose tissue. In this study, co‐overexpression of Pgc‐1α and Mipep upregulated the gene expression of PHOSPHO1. These findings provide new insights into mitochondria‐related mechanisms underlying the effects of caloric restriction in adipocytes.
Mamiko Ishimatsu +9 more
wiley +1 more source
Cytochrome c-554 from Methylosinus trichosporium OB3b; a protein that belongs to the cytochrome c2 family and exhibits a HALS-Type EPR signal. [PDF]
PLoS ONE, 2011 A small soluble cytochrome c-554 purified from Methylosinus trichosporium OB3b has been purified and analyzed by amino acid sequencing, mass spectrometry, visible, CD and EPR spectroscopies.
Espen Harbitz, K Kristoffer Andersson
doaj +1 more source