607-14-7Relevant articles and documents
Photoinitiated Electron Transfer between Cytochrome c and Cytochrome c Oxidase Using a Novel Uroporphyrin/NADH Reducing System
Larsen, Randy W.,Winkler, Jay R.,Chan, Sunney I.
, p. 8023 - 8027 (1992)
We have employed a novel photoreduction system to investigate the electron-transfer reaction between cytochrome c and cytochrome c oxidase.In this system, the photogenerated uroporphyrin triplet state is quenched through electron transfer to ferricytochrome c.The corresponding uroporphyrin ?-cation radical is rapidly reduced by nicotonamid adenine dinucleotide (NADH) resulting in the in situ generation of ferrocytochrome c.In the presence of cytochrome c oxidase, cytochrome c is reoxidized biphasically while the corresponding reduction of cytochrome a appears to be monophasic.In addition, the fast-phase rate constants are dependent upon the concentration of cytochrome c oxidase giving a first-order intracomplex electron-transfer rate constant, (ket), of 1829 +/-248 s-1.The ratio of electron transferred from ferrocytochrome c to cytochrome a is 1:1 indicating that cytochrome a is the ultimate acceptor of the electrons.
Direct assay of enzymes in heme biosynthesis for the detection of porphyrias by tandem mass spectrometry. Uroporphyrinogen decarboxylase and coproporphyrinogen III oxidase
Wang, Yuesong,Gatti, Paula,Sadilek, Martin,Scott, C. Ronald,Turecek, Frantisek,Gelb, Michael H.
, p. 2599 - 2605 (2008/09/20)
We report new assays of enzymes uroporphyrinogen decarboxylase (UROD) and coproporphyrinogen III oxidase (CPO) in the heme biosynthetic pathway. The assays were developed for use in clinical diagnostics of inherited disorders porphyria cutanea tarda and hereditary coproporphyria, respectively. Electrospray ionization tandem mass spectrometry is used to monitor the decarboxylation of pentaporphyrinogen I or uroporphyrinogen III catalyzed by UROD and to determine the enzyme activity in human erythrocytes by measuring the production of coproporphyrinogen I or III. The Km value for pentaporphyrinogen I was measured as 0.17 ± 0.03 μM. A mass spectrometric assay was also developed for the two-step decarboxylative oxidation of coproporphyrinogen III to protoporphyrinogen IX catalyzed by CPO in mitochondria from human lymphocytes (Km = 0.066 ± 0.009 μM). The assays show good reproducibility, use simple workup by liquid-liquid extraction of enzymatic products, and employ commercially available substrates and internal standards.
Studies on the formation of porphyrinogens from monopyrroles in presence of the enzymes PBG deaminase and/or Uro'gen III synthase
Pichon-Santander, Clotilde,Ian Scott
, p. 8669 - 8672 (2007/10/03)
The substrate-specificities of two enzymes in the biosynthetic pathway to vitamin B12, PBG deaminase and Uro'gen III synthase, which are involved in the formation of Uro'gen III from the pyrrole PBG, are investigated for the preparation of Uroporphyrin analogs. Both enzymes display strong substrate-specificity. However, tetramerization of pyrroles with carboxylate β-substituents in mildly basic buffer represents the best and most rapid route to a family of Uro I analogs for enzymatic activity studies.