Science 142:681–682 Shuvalov VA, Klimov VV, Krakhmaleva IN, Krasnovsky AA (1976) Phototransformation of bacteriopheophytin in reaction centers of R. rubrum and C. minutissium. Dokl AN SSSR (in Russ) 227:984–987 Shuvalov VA, Nuijs AM, van Gorkom HJ, Smit HWJ, Duysens LNM (1986) Picosecond absorption changes upon selective excitation of the primary electron donor P-700 in photosystem I. Biochim Biophys Acta 850:319–323CrossRef Wasielewski MR, Fenton JM, Govindjee (1987) The rate of formation of P700+ A o − in photosystem I particles from spinach measured by picosecond transient absorption spectroscopy. Photosynth Res 12:181–190PubMedCrossRef

Footnotes 1 A pdf file of this lecture see more “Honoring Alexander A. Krasnovsky by Govindjee (2013)” is available at a web site; it is the 16th entry under Announcements at < http://​www.​life.​illinois.​edu/​govindjee>. Further, right below it is a pdf file showing many group photographs of Krasnovsky, provided by Armin Meister to Govindjee; these photographs were taken, during 1967—1981, at conferences of Council of Mutual Economic Assistance (COMECON or CMEA).”
“Introduction The water oxidation AZD9291 reaction of oxygenic photosynthesis is catalysed by the photosystem II (PSII) complex located in the thylakoid

membranes of chloroplasts and cyanobacteria. Crystal structures of monomeric and dimeric oxygen-evolving PSII complexes isolated from the thermophilic cyanobacteria Thermosynechococcus

vulcanus and Thermosynechococcus elongatus have been determined (Kamiya and Shen 2003; Ferreira et al. 2004; Loll et al. 2005; Guskov et al. 2009; Broser et al. 2010; Umena et al. 2011). Each PSII monomer contains about 20 subunits, depending on the preparation, most of which are integral to the membrane (reviewed by Müh et al. 2008). In the case of cyanobacteria three extrinsic proteins (PsbO, PsbU and PsbV) are attached to the lumenal CYT387 research buy surface of the crystallised complex where in vivo they help to shield the Mn4CaO5 oxygen-evolving complex from aberrant reduction (Shen et al. 1998). A different set of proteins (PsbO, PsbP, PsbQ and PsbR) is associated with PSII in green algae Branched chain aminotransferase and higher plant chloroplasts, but their binding sites remain unclear (reviewed by Bricker et al. 2012). For red algae and diatoms, an intermediate situation exists in which a PsbQ-like subunit (termed PsbQ’) is present in addition to the PsbO, PsbU and PsbV subunits, while a fifth subunit, Psb31, is also found in diatoms (reviewed by Enami et al. 2008). PsbP-like and PsbQ-like proteins are also expressed in higher plant chloroplasts, but they have roles outside PSII. For instance, two PsbQ-like proteins are components of the thylakoid NADH dehydrogenase-like (NDH) complex in Arabidopsis (Yabuta et al. 2010). Homologues of PsbP and PsbQ are also found in cyanobacteria (Thornton et al. 2004).