. Currents in biochemical research, 1956; twenty-seven essays charting the present course of biochemical research and considering the intimate relationship of biochemistry to medicine, physiology, and biology. Biochemistry -- Research. HENRY R. MAHLER Interaction between Flavoprotein and Cytochromes We might then summarize and extend the possible means of interaction between enzymes at the flavoprotein and those at the cytochrome level in the following manner (see Figure 3). Probably the most significant feature of this scheme is its inherent complexity. Instead of one straight-line path from
. Currents in biochemical research, 1956; twenty-seven essays charting the present course of biochemical research and considering the intimate relationship of biochemistry to medicine, physiology, and biology. Biochemistry -- Research. HENRY R. MAHLER Interaction between Flavoprotein and Cytochromes We might then summarize and extend the possible means of interaction between enzymes at the flavoprotein and those at the cytochrome level in the following manner (see Figure 3). Probably the most significant feature of this scheme is its inherent complexity. Instead of one straight-line path from substrate to oxygen we find the electrons traveling several paths in parallel. |i ^CYTOCHROMES b'' | l 'CYTOCHROME OXIDASg* \ OF f. Figure 3. This is not to suggest that all paths will be operative at any one time. During any one set of physiological parameters probably only one of the several alternatives will actually be in use. The switches are set for this particular alternative. But the other possibilities are always present. Under the influence of metabolic controls at one or several junction points an alternate path may become obligatory. Thus the electrons may be diverted from say a relatively slow but energetically efficient to a more rapid but ineflficient route, for example, during uncoupling of oxidative phosphorylation (20). Another feature worth noting may be that quinones (, vitamin K) and cytochrome c lie on parallel paths. The scheme also illustrates a second point: electron transfers from the flavin stage onward, at least in the native 264. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Green, David Ezra, 1910-. New York, Interscience Publishers
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