Results 11 to 20 of about 3,386 (219)
Mechanistics of pH-Dependent Sulfmyoglobin Formation: Spin Control and His64 Proton Relay
Journal of ChemistryThe chemistry of hydrogen sulfide (H2S) has been directed towards physiologically relevant hemeproteins, including myoglobin, hemoglobin, and other similar proteins.
Angel D. Rodriguez-Mackenzie +4 more
doaj +2 more sources
A natural heme deficiency exists in biology that allows nitric oxide to control heme protein functions by regulating cellular heme distribution. [PDF]
Bioessays, 2023 We hypothesize that tissues exist naturally in a heme‐deficient condition that limits the heme content and functions of heme proteins. The nitric oxide (NO) that is made in our tissues can control cell heme availability in a bimodal way, and so regulate heme protein functions in health and disease.
Stuehr DJ +5 more
europepmc +2 more sources
The Purity of Two Commercial Hemeproteins. [PDF]
Acta Chemica Scandinavica, 1985 Kalidas Paul +5 more
openalex +3 more sources
Implication to the catalytic process of hemeproteins [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2011 Y. Ohgo +8 more
openalex +2 more sources
Biomimetic chemistry of hemeproteins.
The Keio Journal of Medicine, 1989 Hemeproteins play important physiological roles for an oxygen metabolism in living organisms. Their functions are divided to three main groups, i) hemoglobins, myoglobins and the cytochromes which function by transporting and storing dioxygen and electrons; ii) catalase and peroxidases which are activated by hydrogen peroxide, iii) cytochrome oxidase ...
David Dolphin
openalex +4 more sources
How does NO activate hemeproteins? [PDF]
FEBS Letters, 1994 NO was reported to activate guanylate cyclase and, recently, prostaglandin H synthase. NO interaction with the heme component in different hemeproteins is determined by ligand property, electronic configuration of the heme iron and the specific effects contributed by the protein structure.
Ah‐Lim Tsai
openalex +4 more sources
Light‐Induced Pulsed EPR Dipolar Spectroscopy on a Paradigmatic Hemeprotein [PDF]
ChemPhysChem, 2019 AbstractLight‐induced pulsed EPR dipolar spectroscopic methods allow the determination of nanometer distances between paramagnetic sites. Here we employ orthogonal spin labels, a chromophore triplet state and a stable radical, to carry out distance measurements in singly nitroxide‐labeled human neuroglobin.
Maria Giulia Dal Farra +8 more
openalex +6 more sources
Angewandte Chemie, Volume 135, Issue 35, August 28, 2023., 2023 Computational modelling was employed to rationally guide protein engineering toward controlling the accessible conformations of a key lactone‐carbene (LAC) intermediate in the enzyme active site by installing a new H‐bond anchoring point. This H‐bonding interaction controls the relative orientation of the fleeting carbene intermediate, orienting it for
Carla Calvó‐Tusell +4 more
wiley +2 more sources
Chemoselective Caging of Carboxyl Groups for On‐Demand Protein Activation with Small Molecules
Angewandte Chemie, Volume 135, Issue 22, May 22, 2023., 2023 The caging of amino acid side chains can provide exquisite control of protein function. The first chemical caging of carboxyl groups (Asp and Glu) in enzymic active sites is reported. Caging of a heme propionate in a protein was also feasible by this approach based on esterification with a tuned diazo compound.
Yana D. Petri +2 more
wiley +2 more sources
Rhabdomyolysis as cause, consequence, or mimicker of myocardial infarction: A case report
Clinical Case Reports, Volume 11, Issue 11, November 2023., 2023 Key Clinical Message A timely diagnosis is essential to start appropriate therapy and to reduce risks of life‐threatening complications of rhabdomyolysis. Some cases can undergo differential diagnosis with other clinical conditions, e.g., myocardial infarction.
Marina Nasello +11 more
wiley +1 more source