Results 71 to 80 of about 339,218 (339)
Heme Oxygenase-1 Expression Affects Murine Abdominal Aortic Aneurysm Progression. [PDF]
, 2016 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is a cytoprotective enzyme upregulated in the vasculature by increased flow and inflammatory stimuli.
Azuma, Junya +13 more
core +2 more sources
Evidence for Heme Oxygenase Activity in a Heme Peroxidase
Biochemistry, 2009 The heme peroxidase and heme oxygenase enzymes share a common heme prosthetic group but catalyze fundamentally different reactions, the first being H(2)O(2)-dependent oxidation of substrate using an oxidized Compound I intermediate, and the second O(2)-dependent degradation of heme.
Badyal, SK +9 more
openaire +5 more sources
Advanced Functional Materials, EarlyView.Rationally‐designed advanced carbon‐based single‐atom catalysts with isolated CuN2O2 active sites anchored in N,O‐doped porous carbon facilitate water dissociation and nitrate reduction, accelerating proton supply for efficient electrosynthesis of ammonia.
Yan Li +14 more
wiley +1 more source
Import of cytochrome c into mitochondria [PDF]
, 1989 The covalent attachment of heme to apocytochrome c, and therefore the import of cytochrome c into mitochondria, is dependent on both NADH plus a cytosolic cofactor that has been identified to be FMN or FAD.
Neupert, Walter, Nicholson, Donald W.
core
A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria [PDF]
, 1988 The nuclear cyt-2-1 mutant of Neurospora crassa is characterized by a gross deficiency of cytochrome c (Bertrand, H., and Collins, R. A. (1978) Mol. Gen. Genet. 166, 1-13).
Drygas, Mariola E. +4 more
core +1 more source
Deciphering Tryptophan Oxygenation: Key Modulators of 2-Oxindole Formation in MarE. [PDF]
Angew Chem Int Ed EnglThis study reveals that MarE, a heme‐dependent aromatic oxygenase, favors dioxygenation of β‐methyl‐l‐tryptophan in the absence of ascorbate and demonstrates how structural and redox tuning shifts its reactivity toward selective monooxygenation, yielding a 2‐oxindole scaffold. These findings offer new insights into enzyme‐controlled indole oxidation in
Nguyen RC, Shin I, Liu A.
europepmc +3 more sources
Advanced Healthcare Materials, Volume 14, Issue 7, March 14, 2025.This review highlights emerging bioengineering strategies for treating neointimal hyperplasia in the peripheral vasculature, focusing on approaches that promote re‐endothelialization, modulate smooth muscle cell phenotype, reduce inflammation, mitigate oxidative stress, and optimize biomechanical compliance.
Nikita Wilson John +5 more
wiley +1 more source
Biogenesis of mitochondrial c-type cytochromes [PDF]
, 1990 Cytochromesc andc 1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space;
Gonzales, Daniel H., Neupert, Walter
core +2 more sources
Advanced Healthcare Materials, Volume 14, Issue 7, March 14, 2025.BX‐001N, a polyethylene glycol‐conjugated bilirubin 3α nanoparticle, is the first GMP‐grade, synthetic bilirubin‐based nanomedicine. It effectively attenuates acute renal injury, facilitates subacute renal recovery, and suppresses chronic fibrosis after renal ischemia/reperfusion injury via anti‐oxidant and immune‐modulating activity.
Ji‐Jing Yan +13 more
wiley +1 more source
Linking Conformation Change to Hemoglobin Activation Via Chain-Selective Time-resolved Resonance Raman Spectroscopy on Protoheme/Mesoheme Hybrids [PDF]
, 2009 Time-resolved Resonance Raman spectra are reported for Hb tetramers, in which the αand β chains are selectively substituted with mesoheme. The Soret absorption band shift in meso- relative to protoheme permits chain-selective excitation of heme RR ...
Balakrishnan, Gurusamy +5 more
core +2 more sources