1K1000 Replacement of axial ligand by carbon monoxide in DvMF cytochrome c_3
نویسندگان
چکیده
منابع مشابه
Site-directed mutagenesis of tetraheme cytochrome c3. Modification of oxidoreduction potentials after heme axial ligand replacement.
The nature of the axial ligands of a heme group is an important factor in maintaining the oxidation-reduction potential of a c-type cytochrome. Cytochrome c3 from Desulfovibrio vulgaris Hildenborough contains four bis-histidinyl coordinated hemes with low oxidation-reduction potentials. Site-directed mutagenesis was used to generate a mutant in which histidine 70, the sixth axial ligand of heme...
متن کاملVictim of carbon monoxide poisoning identified by carbon monoxide oximetry.
BACKGROUND Carbon monoxide (CO) is known as a leading cause of unintentional poisoning death in many countries. Diagnosis is usually made by measuring carboxyhemoglobin (COHb), but due to the non-specific symptoms, the crucial step is considering CO poisoning. A possible solution might be screening emergency department (ED) patients. A cutaneous sensor that measures oxygen and CO saturation sim...
متن کاملThe Reaction of Cytochrome Oxidase with Carbon Monoxide*
The participation of molecular oxygen in biological oxidations is catalyzed by an enzyme which has been called-a variety of names starting with Atmungsfemzent by Warburg (18) to the currently employed term of cytochrome oxidase proposed by Keilin and Hartree (11). Presumably the enzyme functions by first combining with molecular oxygen and then becoming oxidized by it. As first shown by Warburg...
متن کاملBiological signaling by carbon monoxide and carbon monoxide-releasing molecules.
Carbon monoxide (CO) is continuously produced in mammalian cells during the degradation of heme. It is a stable gaseous molecule that reacts selectively with transition metals in a specific redox state, and these characteristics restrict the interaction of CO with defined biological targets that transduce its signaling activity. Because of the high affinity of CO for ferrous heme, these targets...
متن کاملReactions of cytochrome oxidase with oxygen and carbon monoxide.
Although spectrophotometric determinations of steady states together with turnover rates have allowed Chance (1952) to calculate that the rate of reaction of reduced cytochrome oxidase with oxygen must be about 107M-1 sec.-', no direct measurements of this rate appear to have been reported. This is due to the difficulty of obtaining the enzyme in a form which can be studied spectrophotometrical...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2002
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.42.s60_4