By Nord F F (ed)
Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative reports of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unequalled view of the historic improvement of enzymology. The sequence bargains researchers the most recent figuring out of enzymes, their mechanisms, reactions and evolution, roles in advanced organic method, and their program in either the laboratory and undefined. each one quantity within the sequence positive aspects contributions by way of prime pioneers and investigators within the box from around the globe. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of subject matters and lengthy historic pedigree, Advances in Enzymology and similar components of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition through any scientist drawn to the invention of an enzyme, its homes, and its purposes.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 30
In the presence of DCMU, both red and far-red light caused an oxidation of cyt 553 and cyt 559. I n the mutant strain which Iacked cyt 553 (ac-206), red light induced a reduction of cyt 559. In the strains which lacked cyt 559 (ac-l/fl and ac-115), no light-induced absorbance changes were noted until the chloroplast fragments (and cyt 553) were reduced with ascorbate. Then both red and far-red light caused an oxidation of cyt 553. From these results Levine and Gorman (163) concluded t ha t in Chlamydomonas, cyt 553 and cyt 559 are electron carriers acting in series between the pigment systems, with cyt 559 closer t o pigment system 2.
No significant absorbancy changes were observed in isolated chloroplasts in the absence of added ferredoxin. On addition of purified ferredoxin, 640 mp light reduced the ferredoxin, and the reduced ferredoxin was reoxidized in the dark. Addition of NADP+ to the illuminated chloroplast suspension resulted in a rapid reoxidation of ferredoxin, so that the steady-state level of added ferredoxin was almost completely oxidized. When all the NADP+ was reduced, ferredoxin was reduced again. The oxidation of reduced ferredoxin by NADP+ was completely inhibited by the antibody to the flavoprotein ferredoxinNADP reductase.
Because of the biphasic nature of the fluorescence rise curve it was assumed that the primary quencher Q, after being reduced in the light, was reoxidized by another intermediate P (178). The Japanese workers (192) postulated two such intermediates. , the number of quanta required to convert (Q P) into (QP-), assuming that 1 equivalent of Q was reduced for 2 einsteins of green light absorbed. Experimental support for the latter assumption was provided by measuring the number of quanta of green light required t o completely reduce small amounts of an added oxidant, ferrieyanide (151,178).