Results 1 to 10 of about 60,609 (146)

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

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

Polystyrene Degradation by Exiguobacterium sp. RIT 594: Preliminary Evidence for a Pathway Containing an Atypical Oxygenase

open access: yesMicroorganisms, 2022
The widespread use of plastics has led to their increasing presence in the environment and subsequent pollution. Some microorganisms degrade plastics in natural ecosystems and the associated metabolic pathways can be studied to understand the degradation
Anutthaman Parthasarathy   +6 more
doaj   +1 more source

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

Structure and mutation of deoxypodophyllotoxin synthase (DPS) from Podophyllum hexandrum

open access: yesFrontiers in Catalysis, 2023
Deoxypodophyllotoxin synthase (DPS) is a 2-oxoglutarate (2-OG) dependent non-heme iron (II) dioxygenase that catalyzes the stereoselective ring-closing carbon-carbon bond formation of deoxypodophyllotoxin from the aryllignan (−)-yatein ...
Zoe Ingold   +3 more
doaj   +1 more source

Early Steps in the Biosynthetic Pathway of Rishirilide B

open access: yesMolecules, 2020
The biological active compound rishirilide B is produced by Streptomyces bottropensis. The cosmid cos4 contains the complete rishirilide B biosynthesis gene cluster.
Philipp Schwarzer   +10 more
doaj   +1 more source

The Naphthalene Catabolic Genes of Pseudomonas putida BS3701: Additional Regulatory Control

open access: yesFrontiers in Microbiology, 2020
Pseudomonas microorganisms are used for bioremediation of soils contaminated with petroleum hydrocarbons. The overall remediation efficiency is largely dependent on the presence of macro- and micronutrients.
Irina Pozdnyakova-Filatova   +5 more
doaj   +1 more source

Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates

open access: yeseLife, 2019
Human and other animal cells deploy three closely related dioxygenases (PHD 1, 2 and 3) to signal oxygen levels by catalysing oxygen regulated prolyl hydroxylation of the transcription factor HIF. The discovery of the HIF prolyl-hydroxylase (PHD) enzymes
Matthew E Cockman   +10 more
doaj   +1 more source

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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