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The structure of cytochrome b5 reductase, the enzyme that converts methemoglobin to hemoglobin. [1]Methemoglobin (British: methaemoglobin, shortened MetHb) (pronounced "met-hemoglobin") is a hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe 3+ state, not the Fe 2+ of normal hemoglobin.
Cytochrome b5 reductase is a prevalent topic in research and clinical tests to understand the additional functions of the enzyme in other metabolic pathways in the body. Mice and flies are common model organisms used to test for the relationship of cytochrome b5 reductase with the overall health of living organisms.
Normally, methemoglobin levels are <1%, as measured by the CO-oximetry test. Elevated levels of methemoglobin in the blood are caused when the mechanisms that defend against oxidative stress within the red blood cell are overwhelmed and the oxygen carrying ferrous ion (Fe 2+) of the heme group of the hemoglobin molecule is oxidized to the ...
In human blood a trace amount of methemoglobin is normally produced spontaneously; the enzyme methemoglobin reductase is responsible for converting methemoglobin back to hemoglobin. [ 23 ] [ 24 ] Methemoglobinemia can be hereditary but more commonly occurs as a side effect of certain medications or by abuse of recreational drugs .
It's also heavily involved in many oxidation and reduction reactions, such as the reduction of methemoglobin to hemoglobin. [10] Of the two forms of NADH-cytochrome b5 reductase, the membrane-bound form exists mainly on the cytoplasmic side of the endoplasmic reticulum and functions in desaturation and elongation of fatty acids , in cholesterol ...
Nitro blue tetrazolium is used in a diagnostic test, in particular, for chronic granulomatous disease, a disease in which there is a defect in NADPH oxidase; therefore, the phagocyte is unable to make the reactive oxygen species or radicals required for bacterial killing, resulting in bacteria thriving within the phagocyte. The higher the blue ...
Cytochrome P450 reductase (also known as NADPH:ferrihemoprotein oxidoreductase, NADPH:hemoprotein oxidoreductase, NADPH:P450 oxidoreductase, P450 reductase, POR, CPR, CYPOR) is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 [5] and other heme proteins including heme oxygenase in the endoplasmic reticulum [6] of the eukaryotic cell.
1728 18104 Ensembl ENSG00000181019 ENSMUSG00000003849 UniProt P15559 Q64669 RefSeq (mRNA) NM_001286137 NM_000903 NM_001025433 NM_001025434 NM_008706 RefSeq (protein) NP_000894 NP_001020604 NP_001020605 NP_001273066 NP_032732 Location (UCSC) Chr 16: 69.71 – 69.73 Mb Chr 8: 108.11 – 108.13 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse NAD(P)H dehydrogenase [quinone] 1 is an ...