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Electron buffering

These measurements indicate that it is not possible to identify a single value of pe surrounding the O2/H2S interface in the environment. Redox couples do not respond to the pe of the environment with the same lability as hydrogen ion donors and acceptors. There is no clear electron buffer capacity other than the most general states of "oxygen containing" or "H2S containing." The reason for the vast differences in pec in the oxic waters is the slow oxidation kinetics of the reduced forms of the redox couples. The reduced species for which the kinetics of oxidation by O2 has been most widely studied is Mn. This oxidation reaction... [Pg.432]

The mechanism and sequence of events that control delivery of protons and electrons to the FeMo cofactor during substrate reduction is not well understood in its particulars.8 It is believed that conformational change in MoFe-protein is necessary for electron transfer from the P-cluster to the M center (FeMoco) and that ATP hydrolysis and P release occurring on the Fe-protein drive the process. Hypothetically, P-clusters provide a reservoir of reducing equivalents that are transferred to substrate bound at FeMoco. Electrons are transferred one at a time from Fe-protein but the P-cluster and M center have electron buffering capacity, allowing successive two-electron transfers to, and protonations of, bound substrates.8 Neither component protein will reduce any substrate in the absence of its catalytic partner. Also, apoprotein (with any or all metal-sulfur clusters removed) will not reduce dinitrogen. [Pg.235]

To summarize, the special bonding characteristics of 7r-acceptor ligands in organotransition metal compounds enable these complexes to coordinate small molecules such as ethylene, CO, and H2 and also provide an electronic buffer system to facilitate changes of metal oxidation state and coordination... [Pg.398]

The electron donor to Chl+ in PSI of chloroplasts is the copper protein plastocyanin (Fig. 2-16). However, in some algae either plastocyanin or a cytochrome c can serve, depending upon the availability of copper or iron.345 Both QA and QB of PSI are phylloquinone in cyanobacteria but are plastoquinone-9 in chloroplasts. Mutant cyanobacteria, in which the pathway of phylloquinone synthesis is blocked, incorporate plasto-quinone-9 into the A-site.345a Plastoquinone has the structure shown in Fig. 15-24 with nine isoprenoid units in the side chain. Spinach chloroplasts also contain at least six other plastoquinones. Plastoquino-nes C, which are hydroxylated in side-chain positions, are widely distributed. In plastoquinones B these hydroxyl groups are acylated. Many other modifications exist including variations in the number of iso-prene units in the side chains.358 359 There are about five molecules of plastoquinone for each reaction center, and plastoquinones may serve as a kind of electron buffer between the two photosynthetic systems. [Pg.1314]

The unique electron buffer function of the Pt-Pt bond allows Pt111 dimers to exhibit various reactivities. [Pg.449]

The Electronic Buffer Effect in Oxo-metal-mono(dithiolenes) / 128... [Pg.111]


See other pages where Electron buffering is mentioned: [Pg.245]    [Pg.288]    [Pg.549]    [Pg.204]    [Pg.281]    [Pg.128]    [Pg.137]    [Pg.526]    [Pg.128]    [Pg.137]    [Pg.526]   
See also in sourсe #XX -- [ Pg.235 ]




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