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Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source').
In the plant-like family of FNRs, selective evolutionary pressure has led to differences in the catalytic efficiency of FNRs in photosynthetic and nonphotosynthetic organisms. Electron transfer by FNR is a rate limiting step in photosynthesis, so the plastidic FNR in plants have evolved to be highly efficient. [8]
Some NAD is converted into the coenzyme nicotinamide adenine dinucleotide phosphate (NADP), whose chemistry largely parallels that of NAD, though its predominant role is as a coenzyme in anabolic metabolism. In the name NAD +, the superscripted plus sign indicates the positive formal charge on one of its nitrogen atoms. A biological coenzyme ...
This dimer is called a special pair because of its fundamental role in photosynthesis. This special pair is slightly different in PSI and PSII reaction centers. In PSII, it absorbs photons with a wavelength of 680 nm, and is therefore called P680. In PSI, it absorbs photons at 700 nm and is called P700. In bacteria, the special pair is called ...
Ferredoxin, also known as an NADP+ reductase, is an enzyme that catalyzes the reduction reaction. It is easy to oxidize NADPH but difficult to reduce NADP +, hence a catalyst is beneficial. Cytochromes are conjugate proteins that contain a haem group. [5] The iron atom from this group undergoes redox reactions:
Photosystem I operates with the functions of producing NADPH, the reduced form of NADP + (Fd 2-red + NADH + 2 NADP + + H + = Fd ox + NAD + + 2 NADPH.), at the end of the photosynthetic reaction through electron transfer, and of providing energy to a proton pump and eventually ATP, for instance in cyclic electron transport.
P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, p. 959-962. Valverde F, Losada M, Serrano A (1997). "Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803". J.
Rather, NADP-ME was directly transformed from a C 3 species in photosynthesis, and even earlier origins from an ancient cystolic ancestor. In the cytosol, the enzyme existed as a series of housekeeping isoforms purposed towards a variety of functions including malate level maintenance during hypoxia, microspore separation, and pathogen defense.