| Evolution of Chlorophyll Biosynthesis—The Challenge to Survive Photooxidation Cell, Volume 86, Issue 5, 6 September 1996, Pages 703-705 Steffen Reinbothe, Christiane Reinbothe, Klaus Apel and Nikolai Lebedev Full Text | PDF (56 kb) |
| Does a light-harvesting protochlorophyllide a/b-binding protein complex exist? Trends in Plant Science, Volume 5, Issue 1, 1 January 2000, Pages 40-44 Gregory A Armstrong, Klaus Apel and Wolfhart Rüdiger Abstract Recent studies have led to speculation that a novel light-harvesting protochlorophyllide /-binding protein complex (LHPP) might exist in dark-grown angiosperms. Structurally, it has been suggested that LHPP consists of a 5:1 ratio of dark-stable ternary complexes of the light-dependent NADPH: protochlorophyllide oxidoreductases A and B containing nonphotoactive protochlorophyllide and photoactive protochlorophyllide , respectively. Functionally, LHPP has been hypothesized to play major roles in establishing the photosynthetic apparatus, in protecting against photo-oxidative damage during greening, and in determining etioplast inner membrane architecture. However, the LHPP model is not compatible with other studies of the pigments and the pigment–protein complexes of dark-grown angiosperms. Protochlorophyllide , which is postulated to be the major light-harvesting pigment of LHPP, has, for example, never been detected in etiolated seedlings. This raises the question: does LHPP exist? Abstract | Full Text | PDF (108 kb) |
| Making light work of enzyme catalysis: protochlorophyllide oxidoreductase Trends in Biochemical Sciences, Volume 30, Issue 11, 1 November 2005, Pages 642-649 Derren J. Heyes and C. Neil Hunter Abstract In the chlorophyll biosynthetic pathway, the enzyme protochlorophyllide oxidoreductase (POR) catalyses a key light-driven reaction that triggers a profound transformation in plant development. Because POR is activated by light, it can provide information on the way in which light energy can be harnessed to power enzyme reactions and it presents us with a unique opportunity to study catalysis at low temperatures and on ultrafast timescales that are not accessible for most analyses of enzyme function. Recent advances in our understanding of the catalytic mechanism of POR illustrate why it is an important generic model for studying enzyme catalysis and reaction dynamics. Abstract | Full Text | PDF (509 kb) |
Copyright © 1972 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 12, Issue 7, 749-763, 1 July 1972
doi:10.1016/S0006-3495(72)86119-8
General Photophysics and Photochemistry
A.A. Krasnovsky
In this paper the recent research from our laboratory is reviewed. Short fragments of the photochemical electron transfer chain of photosynthesis were reproduced in aqueous detergent solutions or in organic solvents. The function of photosystem I is reproduced in a ternary system of chlorophylls, electron donors (dienols, sulfhydryl compounds, hydrazine, etc.), and electron acceptors (viologens, nicotinamide-adenine dinucleotide [NAD], flavines, etc.). Chlorophyll-photosensitized reduction of viologens in some cases is activated by oxygen at the expense of active reductants formed during the photosensitized oxidation of an initial electron donor (thiourea). Chlorophyll-photosensitized oxidoreduction of cytochromes is activated by flavines, viologens, vitamin K derivatives, and some other redox systems (cofactors of cyclic photophosphorylation). The primary mechanism of the reactions studied depends on the reversible chlorophyll photooxidoreduction. In binary systems, chlorophyll (monomeric or aggregated) and electron donor or electron acceptor, reversible photoreduction or photooxidation is observed. Irreversible bacteriochlorophyll oxidation leads to the formation of chlorophyll and protochlorophyll analogues; irreversible protochlorophyll photoreduction results in chlorophyll-like pigment appearance. The photodisaggregation of chlorophyll was observed. The models of photosystem II studied were the photochemical oxygen evolution in aqueous solutions of electron acceptors (ferric compounds, quinone), photosensitized in the near UV part of the spectrum by inorganic semiconductors (tungsten, titanium, and zinc oxides). All reactions described are based on electron (hydrogen) transfer photosensitized by pigment system.