About: Steady-state and Transient Kinetics ofEscherichia coliNitric-oxide Dioxygenase (Flavohemoglobin)

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About: Steady-state and Transient Kinetics ofEscherichia coliNitric-oxide Dioxygenase (Flavohemoglobin) Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im April 2000 veröffentlicht worden isch (gsw) наукова стаття, опублікована у квітні 2000 (uk) im April 2000 veröffentlichter wissenschaftlicher Artikel (de) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q59599927-EF002F72-B621-429B-9657-447608563F03
publication date	2000-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59599927-238BD2B4-4BA4-4983-9C06-29D039DF65A5
language of work or name	English
cites work	wds:Q59599927-032AFE92-A843-4C6E-8C10-A95173DA5AE4 wds:Q59599927-092FD56D-EF8A-4D95-93C8-C828C3502BE5 wds:Q59599927-0B3F42D6-DD97-4D4E-AF92-11F16827B634 wds:Q59599927-1229C283-0378-41F0-B716-BBF505C2BD7B wds:Q59599927-1D29620C-AC4C-4FD2-9BB6-7576E1835CF2 wds:Q59599927-253876FE-3701-47AE-83B6-7472B4C97D80 wds:Q59599927-42AABCB0-5492-4FEC-ADC1-1E933918A2BD wds:Q59599927-452752CC-86CC-4564-A920-B5FCF36E00DF wds:Q59599927-485C35D0-3BBD-46D9-97DE-AE98684DD605 wds:Q59599927-49B733AE-BE6D-49C4-AC06-3DF3D95A2638 wds:Q59599927-502E6A23-54E8-4AAD-A315-1718B60DE322 wds:Q59599927-6C4FC50C-E683-488D-8A01-EB992BA09325 wds:Q59599927-70325458-9178-4AD4-9596-17C3D17BFFE9 wds:Q59599927-7441352B-25C9-4073-86F5-8146D2DF0A77 wds:Q59599927-745930C5-37D3-42D1-9BD1-59B7A2A1FE04 wds:Q59599927-7470DDA1-AB82-4D76-AF0D-4C44A428C7F5 wds:Q59599927-77BDC5E2-3DE6-4EF1-85CD-18F84ECD95C4 wds:Q59599927-79310826-81E8-4E15-B61D-F5E148A5FA13 wds:Q59599927-7D365561-8D83-402A-9813-90CED229BEB6 wds:Q59599927-7D942ACB-723A-46A6-A69A-AF57E2267171 wds:Q59599927-84A3FAB6-671B-433D-B935-F6334FF027A6 wds:Q59599927-85DABA94-F09D-40A5-BE15-32DB181F6EEE wds:Q59599927-8862BBBF-8766-4235-96F4-536CA4928E03 wds:Q59599927-8FB52C38-5E99-4181-A37E-B4548671B277 wds:Q59599927-93B6DF18-B685-4F7D-8193-7FBFAE181861 wds:Q59599927-947327E3-F1F2-46DF-BE65-28ADF8CAD24B wds:Q59599927-9D29C46B-57AD-4CA0-A4E5-57A57CD670A0 wds:Q59599927-9D9EE61B-A1AE-4428-87FC-77E0BA04D5F8 wds:Q59599927-A12B6D1A-6219-4CFC-80F7-25931D7F0490 wds:Q59599927-A13AD11E-13B5-40F9-8891-1CEEDA11E2CB wds:Q59599927-B0CDB62E-FB89-4802-91EC-1C2D16933934 wds:Q59599927-BA837D95-C170-41B0-A5D4-24C022C4F86D wds:Q59599927-C7F40F9D-F9B1-47CE-8748-8E6DA8CCF77C wds:Q59599927-CF5BDED4-9039-4369-8E23-88F6BBFE4824 wds:Q59599927-D0E9E1BE-90EE-4297-BCF1-6C2DA1B8509A wds:Q59599927-D4DF6CEB-8182-48F1-A682-67A8D1690435 wds:Q59599927-D4F5001B-BF29-4462-B48B-72C122732E2B wds:Q59599927-DE7080FB-1D4F-467E-9F50-39889B949800 wds:Q59599927-DFD5BD97-A900-450A-A38A-DAC34A1FE0D9 wds:Q59599927-E4ED630C-44B8-490C-88BC-74B06485487B wds:Q59599927-E5B20CED-00B0-41EC-AD3D-AB2DBF3FF8EE wds:Q59599927-F2268E8D-5F37-4EA0-BE22-27270F517DE1 wds:Q59599927-F5DFB290-C6CD-42CA-925F-19F8E5CCFBCD wds:Q59599927-FA1FB83C-56E7-4DD5-8660-7E807ED2826A wds:Q59599927-FE95F1CE-47E5-46F4-BDF8-EF521978D8EF
cites work	Purification and molecular properties of yeast hemoglobin. Yeast flavohemoglobin is an ancient protein related to globins and a reductase family An oxygen-binding flavohemoprotein from Alcaligenes eutrophus The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases. Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing. Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein. Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp NADH-dependent methemoglobin reductase from the obligate aerobe Vitreoscilla: Improved method of purification and reexamination of prosthetic groups Ascaris haemoglobin is a nitric oxide-activated 'deoxygenase' Hæmoglobin in Fungi: Occurrence of Hæmoglobin in Yeast and the Supposed Stabilization of the Oxygenated Cytochrome Oxidase An enzymatic globin from a marine worm Oxidation of nitrogen oxides by bound dioxygen in hemoproteins Mechanism of NO-induced oxidation of myoglobin and hemoglobin Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin. A brief history of hemoglobins: plant, animal, protist, and bacteria The role of the reactions of .NO with superoxide and oxygen in biological systems: a kinetic approach Nitric oxide sensitivity of the aconitases Nitric oxide dioxygenase: an enzymic function for flavohemoglobin Phospholipid bound to the flavohemoprotein from Alcaligenes eutrophus Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase Nitrosative stress: metabolic pathway involving the flavohemoglobin Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide. The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a "Nitric oxide Releaser," and paraquat and is essential for transcriptional responses to oxidative stress A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide. A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis Role for the Salmonella flavohemoglobin in protection from nitric oxide. Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin Kinetic pathways and barriers for ligand binding to myoglobin A comparison of functional and structural consequences of the tyrosine B10 and glutamine E7 motifs in two invertebrate hemoglobins (Ascaris suum and Lucina pectinata). The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases Mechanisms of cytoplasmic hemoglobin and myoglobin function Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand The oxygenated flavohaemoglobin from Escherichia coli: evidence from photodissociation and rapid-scan studies for two kinetic and spectral forms A Cooperative Oxygen Binding Hemoglobin fromMycobacterium tuberculosis Purification of Rhizobium cytochromes P-450. One-electron oxidation-reduction properties of hepatic NADH-cytochrome b5 reductase Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin

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