Download Subcellular Biochemistry: Volume 8 by Jürgen Oelze (auth.), Donald B. Roodyn (eds.) PDF

By Jürgen Oelze (auth.), Donald B. Roodyn (eds.)

In this quantity of SUBCELLULAR BIOCHEMISTRY we conceal a variety of issues of substantial organic significance and feature persisted in our coverage of letting authors, instead of editors, come to a decision the "natural" size in their articles. therefore, we have now a few brief yet however major contributions, in addition to extra great chapters. we commence with an in depth account by means of 1. Oelze of the composition and improvement of the bacterial photosynthetic gear. a couple of photosynthetic micro organism are mentioned, with specific emphasis at the well-studied Rhodospirillum rubrum and Rhodopseudomonas sphae­ roides. The reader will without doubt be struck by means of the good wealth of knowledge now to be had at the molecular association of the photosynthetic and respi­ ratory structures in those organisms. both very important is our enhanced lower than­ status of the biosynthesis and meeting of those structures. it truly is now more often than not authorised that photosynthetic micro organism are very good version platforms for the examine of bioenergetic strategies. it can be that they're going to develop into both renowned as versions for the examine of membrane biogenesis, and it really is to be was hoping that Oelze's erudite and complete therapy of the topic may also help during this regard.

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Subcellular Biochemistry: Volume 8

During this quantity of SUBCELLULAR BIOCHEMISTRY we disguise quite a lot of themes of substantial organic value and feature endured in our coverage of letting authors, instead of editors, come to a decision the "natural" size in their articles. hence, we've a few brief yet however major contributions, in addition to extra gigantic chapters.

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The polypeptides from preparations of R. capsulata and R. rubrum had molecular weights of 12,000 and 14,000, respectively. A preparation from the blue-green mutant strain R-26 of R. sphaeroides was reported to contain two copies of a polypeptide with a molecular weight of 8500 in association with two molecules of bacteriochlorophyll (Sauer and Austin, 1978). In principle, this result was supported by an analysis of a B875 protein complex solubilized from membranes of wild-type R. , 1980). The protein moiety, however, was shown to be composed of two polypeptides with molecular weights of 12,000 and 8000.

As described above, the major band arises from light-harvesting bacteriochlorophyll, but the minor one at 800 nm is representative of photochemical reaction-center bacteriochlorophyll. When illuminated this band shifts by 5 nm toward shorter wavelengths (blue shift), which can also be seen with isolated reaction-center preparations. In wild-type strains of all of the other species of the Rhodospirillineae with bacteriochlorophyll a, the rather small 800-nm absorption band of reaction-center bacteriochlorophyll is superimposed on the 800-nm band of the second light-harvesting unit (Figures 5, 6).

Light-dependent NAD+ reduction has been observed with whole cells as well as with isolated membrane suspensions from several species of the phototrophic bacteria (reviewed by Knaff, 1978a). , 1971). Keister and Yike (1967a) were the first to demonstrate that NAD+ reduction with succinate could be catalyzed by membrane suspensions, even in the dark, when ATP or PP j was added to the assay system. This supported the postulate of a partially reversible and energy-dependent electron transport from succinate to NAD+ as originally proposed by Bose and Gest (1962).

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