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Oxygenic photosynthesis: EPR study of photosynthetic electron transport and oxygen-exchange, an overview. Cell Biochem Biophys 2019 Mar;77(1):47-59

Date

11/22/2018

Pubmed ID

30460441

Pubmed Central ID

PMC6524781

DOI

10.1007/s12013-018-0861-6

Abstract

In this review, we consider the applications of electron paramagnetic resonance (EPR) methods to the study of the relationships between the electron transport and oxygen-exchange processes in photosynthetic systems of oxygenic type. One of the purposes of this article is to encourage scientists to use the advantageous EPR oximetry approaches to study oxygen-related electron transport processes in photosynthetic systems. The structural organization of the photosynthetic electron transfer chain and the EPR approaches to the measurements of molecular oxygen (O2) with O2-sensitive species (nitroxide spin labels and solid paramagnetic particles) are briefly reviewed. In solution, the collision of O2 with spin probes causes the broadening of their EPR spectra and the reduction of their spin-lattice relaxation times. Based on these effects, tools for measuring O2 concentration and O2 diffusion in biological systems have been developed. These methods, named "spin-label oximetry," include not only nitroxide spin labels, but also other stable-free radicals with narrow EPR lines, as well as particulate probes with EPR spectra sensitive to molecular oxygen (lithium phthalocyanine, coals, and India ink). Applications of EPR approaches for measuring O2 evolution and consumption are illustrated using examples of photosynthetic systems of oxygenic type, chloroplasts in situ (green leaves), and cyanobacteria.

Author List

Tikhonov AN, Subczynski WK

Author

Witold K. Subczynski PhD Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Chloroplasts
Electron Spin Resonance Spectroscopy
Electron Transport
Nitrogen Oxides
Oxidation-Reduction
Oximetry
Oxygen
Photosynthesis
Photosynthetic Reaction Center Complex Proteins
Spin Labels