嗜硫红假单胞菌血红素、非血红素铁及初级光化学相关成分的电子自旋共振表征 - Suppr

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Electron spin resonance characterization of Chromatium D hemes, non-heme irons and the components involved in primary photochemistry.

作者信息

Dutton P L, Leigh J S

出版信息

Biochim Biophys Acta. 1973 Aug 31;314(2):178-90. doi: 10.1016/0005-2728(73)90133-3.

DOI:10.1016/0005-2728(73)90133-3

PMID:4355789

Abstract

摘要

相似文献

Electron spin resonance characterization of Chromatium D hemes, non-heme irons and the components involved in primary photochemistry.嗜硫红假单胞菌血红素、非血红素铁及初级光化学相关成分的电子自旋共振表征

Biochim Biophys Acta. 1973 Aug 31;314(2):178-90. doi: 10.1016/0005-2728(73)90133-3.

The detection and characterization by electron-paramagnetic-resonance spectroscopy of iron-sulphur proteins and other electron-transport components in chromatophores from the purple bacterium Chromatium.用电子顺磁共振光谱法对紫色细菌嗜色菌的载色体中的铁硫蛋白和其他电子传递成分进行检测和表征。

Biochem J. 1974 Feb;138(2):177-83. doi: 10.1042/bj1380177.

Light-induced electron transport in Chromatium strain D. I. Isolation and characterization of Chromatium chromatophores.嗜色菌D菌株中的光诱导电子传递。I.嗜色菌载色体的分离与特性

Biochim Biophys Acta. 1968 Feb 12;153(2):376-96. doi: 10.1016/0005-2728(68)90082-0.

Light-induced electron transport in Chromatium strain D. II. Light-induced absorbance changes in Chromatium chromatophores.嗜色菌D菌株中的光诱导电子传递。II. 嗜色菌载色体中的光诱导吸光度变化。

Biochim Biophys Acta. 1968 Feb 12;153(2):397-417. doi: 10.1016/0005-2728(68)90083-2.

"Super-reduction" of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide.在二甲基亚砜存在下铬高电位铁硫蛋白的“超还原”

Biochem Biophys Res Commun. 1973 Sep 18;54(2):548-54. doi: 10.1016/0006-291x(73)91457-5.

Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 77 degrees K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa.在77K下，氧化还原电位对嗜硫红假单胞菌（Chromatium D）和荚膜红假单胞菌（Rhodopseudomonas gelatinosa）的载色体中细胞色素、细菌叶绿素和类胡萝卜素相互作用的影响

Biochim Biophys Acta. 1971 Jan 12;226(1):63-80. doi: 10.1016/0005-2728(71)90178-2.

Spectral and photochemical properties of subchromatophore fractions derived from carotenoid-deficient Chromatium by triton treatment.通过曲拉通处理从缺乏类胡萝卜素的嗜色菌中获得的亚色素体组分的光谱和光化学性质。

Biochim Biophys Acta. 1971 Mar 2;226(2):341-53. doi: 10.1016/0005-2728(71)90101-0.

Structural organization of the Chromatium vinosum reaction center associated c-cytochromes.嗜硫红假单胞菌反应中心相关c型细胞色素的结构组织

Biochim Biophys Acta. 1978 Sep 7;503(3):524-44. doi: 10.1016/0005-2728(78)90151-2.

A high potential cytochrome c from Chromatium chromatophores.来自嗜色菌色素体的一种高电位细胞色素c。

Biochim Biophys Acta. 1969 Oct 21;189(2):245-55. doi: 10.1016/0005-2728(69)90051-6.

Electron paramagnetic resonance studies on photosynthetic bacteria. I. Properties of photo-induced EPR-signals of Chromatium D.光合细菌的电子顺磁共振研究。I. 嗜硫红假单胞菌光诱导电子顺磁共振信号的特性。

Biochim Biophys Acta. 1968 Feb 12;153(2):427-47. doi: 10.1016/0005-2728(68)90085-6.

引用本文的文献

Interaction between the intermediary electron acceptor (pheophytin) and a possible plastoquinone-iron complex in photosystem II reaction centers.光合作用系统 II 反应中心的中介电子受体（叶绿素）与可能的质体醌-铁复合物之间的相互作用。

Proc Natl Acad Sci U S A. 1980 Dec;77(12):7227-31. doi: 10.1073/pnas.77.12.7227.

Photooxidation of the high-potential iron-sulfur center in chloroplasts.叶绿体中高电位铁硫中心的光氧化作用。

Proc Natl Acad Sci U S A. 1979 Sep;76(9):4417-20. doi: 10.1073/pnas.76.9.4417.

High potential iron-sulfur proteins and their role as soluble electron carriers in bacterial photosynthesis: tale of a discovery.高潜力铁硫蛋白及其在细菌光合作用中作为可溶性电子载体的作用：一个发现的故事。

Photosynth Res. 2005;85(1):115-31. doi: 10.1007/s11120-004-6556-4.

Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans.光诱导电子从高电位铁硫蛋白转移至紫色光合细菌嗜发酵红杆菌光合反应中心的动力学

Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):6998-7002. doi: 10.1073/pnas.93.14.6998.

Cytochrome bc1 complexes of microorganisms.微生物的细胞色素bc1复合物

Microbiol Rev. 1990 Jun;54(2):101-29. doi: 10.1128/mr.54.2.101-129.1990.

Bacterial iron-sulfur proteins.细菌铁硫蛋白

Microbiol Rev. 1979 Sep;43(3):384-421. doi: 10.1128/mr.43.3.384-421.1979.

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