about
Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae.Identification of hemes and related cyclic tetrapyrroles by matrix-assisted laser desorption/ionization and liquid secondary ion mass spectrometry.Noninvasive auto-photoreduction used as a tool for studying structural changes in heme-copper oxidases by FTIR spectroscopyPurification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix.Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. I. The archaeal terminal oxidase supercomplex is a functional fusion of respiratory complexes III and IV with no c-type cytochromes.Molecular and catalytic properties of the aldehyde dehydrogenase of Gluconacetobacter diazotrophicus, a quinoheme protein containing pyrroloquinoline quinone, cytochrome b, and cytochrome c.Regulation of the heme A biosynthetic pathway: differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae.Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology.Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides.Synthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors.One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases.Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersMolecular genetic and protein chemical characterization of the cytochrome ba3 from Thermus thermophilus HB8.The respiratory system and diazotrophic activity of Acetobacter diazotrophicus PAL5.Characterization of a cytochrome a1 that functions as a ubiquinol oxidase in Acetobacter aceti.Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view.Haem O2 can replace haem A in the active site of cytochrome c oxidase from thermophilic bacterium PS3.Hydrazine and hydroxylamine as probes for O2-reduction site of mitochondrial cytochrome c oxidase.Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide.An Escherichia coli cyoE gene homologue in thermophilic Bacillus PS3 encodes a thermotolerant heme O synthase.The caa3 terminal oxidase of Bacillus stearothermophilus. Transient spectroscopy of electron transfer and ligand binding.Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea.The aerobic electron transport system of Eikenella corrodens.Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase.The terminal oxidases of Paracoccus denitrificans.Cytochrome bo from E. coli does not exhibit the same proton transfer characteristics as the bovine cytochrome c oxidase during oxygen reduction.
P2860
Q27935174-A57E3225-3A16-4372-853B-CC02797ADD76Q30835793-97AF4AAA-155D-43C2-8B3B-E30A2DC0399AQ31052473-51E46955-DC36-4F7B-8A15-45DC222CC71AQ33843931-B43B9E15-6B09-4977-BDBF-7C54AC5D45E0Q34062182-0F48F9DD-81C5-42BF-98E1-A62F995DE66AQ34192700-8874C615-3D6A-4760-BC47-F875BE99F0FFQ34866183-55487E27-6665-48C2-9E8C-F3F8D05D9764Q35556410-FFDA262B-3DE2-4420-9E70-AE48B16F3771Q36110645-609D3695-3766-40E8-8B53-0E61BAFB3EF8Q36667724-2368C2D4-310F-4FE4-92B2-E015CE4C54A8Q37252916-F8EA0281-8656-4A1A-9672-AF021C3FFA1FQ37719995-B948C819-AA82-4548-8613-8CA194067DCFQ37727718-C9B72FB6-6CDD-41F1-A719-F97C97317D6AQ38292043-728B614E-BAEB-4638-9F2D-4633822EAE09Q39497955-99BB874F-5545-4FD9-9D6F-194E98D28278Q39929429-CABEB6CB-7322-4446-B8E1-665B4B49D5BEQ40856201-8894A773-ACA0-4A81-9CE8-57B6C9045C97Q41837362-9D21872E-29B3-4BFC-A106-599811354CC7Q41843280-B6BA0208-69E1-4E18-959E-19FAEF354355Q42147739-4B75E484-162A-43F9-BEBE-51AC49A7E9F5Q43023015-C9AA9C81-CED1-4656-A12A-576357091976Q43023905-3193A1D4-BA3E-4810-84DA-091515C2BC15Q43959081-BDA6B870-77C8-4B74-B68D-3850753F2FB5Q44254331-EA096EE9-07C9-407F-AE04-167B4F3071BAQ50515030-CC7F2126-37D5-4DED-A6DA-F135328197BFQ54198432-7B7A471A-805C-4348-9426-12A6109E3993Q54654635-CFDFC68B-71F2-4F5D-8CE8-76AE0E859146
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The heme groups of cytochrome o from Escherichia coli.
@en
The heme groups of cytochrome o from Escherichia coli.
@nl
type
label
The heme groups of cytochrome o from Escherichia coli.
@en
The heme groups of cytochrome o from Escherichia coli.
@nl
prefLabel
The heme groups of cytochrome o from Escherichia coli.
@en
The heme groups of cytochrome o from Escherichia coli.
@nl
P2860
P356
P1476
The heme groups of cytochrome o from Escherichia coli.
@en
P2093
Puustinen A
Wikström M
P2860
P304
P356
10.1073/PNAS.88.14.6122
P407
P577
1991-07-01T00:00:00Z