Results 11 to 20 of about 219,353 (382)

Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2014
Dietary intake of L-carnitine can promote cardiovascular diseases in humans through microbial production of trimethylamine (TMA) and its subsequent oxidation to trimethylamine N-oxide (TMAO) by hepatic flavin-containing monooxygenases.
Bugg, Tim   +6 more
core   +2 more sources

Heme oxygenase-1 deficiency alters erythroblastic island formation, steady-state erythropoiesis and red blood cell lifespan in mice

open access: yesHaematologica, 2015
Heme oxygenase-1 is critical for iron recycling during red blood cell turnover, whereas its impact on steady-state erythropoiesis and red blood cell lifespan is not known. We show here that in 8- to 14-week old mice, heme oxygenase-1 deficiency adversely
Stuart T. Fraser   +13 more
doaj   +2 more sources

STUDIES ON OXYGENASES

open access: hybridJournal of Biological Chemistry, 1957
Osamu Hayaishi   +2 more
openalex   +4 more sources

The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. [PDF]

open access: greenProceedings of the National Academy of Sciences of the United States of America, 1968
R Tenhunen, Harvey S. Marver, R. Schmid
openalex   +2 more sources

Heme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions

open access: yesBiomolecules, 2021
Heme-oxygenase is the enzyme responsible for degradation of endogenous iron protoporphyirin heme; it catalyzes the reaction’s rate-limiting step, resulting in the release of carbon monoxide (CO), ferrous ions, and biliverdin (BV), which is successively ...
Valeria Consoli   +3 more
semanticscholar   +1 more source

The Diverse Roles of Heme Oxygenase-1 in Tumor Progression

open access: yesFrontiers in Immunology, 2021
Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).
Kim Ngan Luu Hoang   +2 more
semanticscholar   +1 more source

Rubber oxygenases [PDF]

open access: yesApplied Microbiology and Biotechnology, 2018
Natural rubber (NR), poly(cis-1,4-isoprene), is used in an industrial scale for more than 100 years. Most of the NR-derived materials are released to the environment as waste or by abrasion of small particles from our tires. Furthermore, compounds with isoprene units in their molecular structures are part of many biomolecules such as terpenoids and ...
Dieter Jendrossek, Jakob Birke
openaire   +2 more sources

Heme Oxygenase Induction Suppresses Hepatic Hepcidin and Rescues Ferroportin and Ferritin Expression in Obese Mice [PDF]

open access: yes, 2017
Hepcidin, a phase II reactant secreted by hepatocytes, regulates cellular iron levels by increasing internalization of ferroportin-a transmembrane protein facilitating egress of cellular iron.
Arefiev, Yevgeniy   +12 more
core   +2 more sources

Custom tuning of Rieske oxygenase reactivity

open access: yesNature Communications, 2023
Rieske oxygenases use a Rieske-type [2Fe-2S] cluster and a mononuclear iron center to initiate a range of chemical transformations. However, few details exist regarding how this catalytic scaffold can be predictively tuned to catalyze divergent reactions.
Jiayi Tian   +5 more
doaj   +1 more source

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