Photo, 1958 Fig  10 Fred Crane’s research group picnic Although

Photo, 1958 Fig. 10 Fred Crane’s research group picnic. Although this photograph was damaged, it Lenvatinib is shown here for historical purposes. Sitting on the ground: children at the picnic. First standing row 3rd from right is Helen Crane; 5th from right is Rita Barr. On the next standing row (just below the very top row), Ron Berezney (wearing glasses) is on the extreme right; 2nd from right is Linda Funk; 3rd from right is the author Fred Crane (wearing checkered shirt); 4th from right is Frank Sun (wearing glasses). On the very top row is Jack Wilson (right above Linda Funk). All others in the photograph are either members of

Crane laboratory or those related to these members. Photo, 1967 Fig. 11 Fred L. Crane (the author) in his office at Purdue University. Photo, 1972 Q-VD-Oph in vivo Fig. 12 Fred and Marilyn Crane at Purdue University (Marilyn was in the Vision Research Group). Photo, 1983 Acknowledgments David Green (of the Enzyme Institute, University of Wisconsin, Madison)

deserves a lot of credit for encouraging my research into PQ when it was not in the mainstream of heart bioenergetics that he was interested in. Further, Karl Folkers deserves credit for interrupting coenzyme Q research to provide analogs of PQ that advanced research in this area. I express my appreciation to my dedicated colleagues who worked on the PQ story with me: Rita Barr, Larry Kegel, selleck chemicals Barbara Ehrlich, Pat Wood, Melva Henninger and H. N. Bhagavan. I thank Govindjee, the founding Historical Corner editor of Photosynthesis Research, for inviting me to write this personal minireview, for constant interaction,

suggestions and editing from its original draft to the final manuscript. I thank Lilli A Davis for her technical assistance with the manuscript. References Allen JF (2002) Plastoquinone redox control of chloroplast thylakoid protein phosphorylation and distribution of excitation energy between photosystems: new discovery, background, implications. Photosynth Res 73:139–148PubMedCrossRef Ambe KS, Crane FL (1960) Studies on the electron transport system. XXVI. Specificity of coenzyme Q and coenzyme Q derivatives. Biochim Biophys Acta 43:30–40PubMedCrossRef Amesz J (1964) Spectrophotometric evidence for the participation of a quinone in photosynthesis of intact blue-green algae. Biochim Biophys Acta 79:257–265PubMedCrossRef Amesz J (1973) The function of plastoquinone in photosynthetic electron transport. Biochim Biophys Acta 301:35–51PubMed Amesz J (1977) Plastoquinone. In: Trebst A, Avron M (eds) Encyclopedia of plant physiology, vol 5. Springer, Berlin, pp 238–246 Austin JR, Frost E, Vidi PA, Kessler F, Staehelin LA (2006) Plastoglobules are lipoprotein subcompartments of the chloroplast that are permanently coupled to the thylakoid membrane and contain biosynthetic enzymes. Plant Cell 18:1693–1703PubMedCrossRef Barber J, Andersson B (1994) Revealing the blueprint of photosynthesis. Nature 370:31–34CrossRef Barr R, Crane FL (1967) Comparative studies on plastoquinones.

Comments are closed.