https://zenodo.org/record/1258475/files/article.pdf

Electron transfers in chemistry and biology

Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy

New spectrophotometric equations for determining chlorophylls a, b, c1 and c2 in higher plants, algae and natural phytoplankton

Infrared spectroscopy of proteins.

The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis. The central part of the complex consists of two subunits, L and M, each of which forms five membrane-spanning helices. We present the first description of the high-resolution structure of an integral membrane protein.

Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

A comparison has been made between Signal I, the photo-electron spin resonance signal associated with the primary light conversion act in photosynthesis, and free-radical signals generated in various chlorophyll species in vitro. The esr signals obtained from chlorophyll·monomer, (Chl·L)+., chlorophyll dimer, (Chl2)+., and chlorophyll oligomer, (Chl2)n+., are broader than Signal I, whereas the chlorophyll-water adduct, (Chl·H2O)n+., gives a signal very much narrower than Signal I. The unusually narrow signal from (Chl·H2O)n+. has been ascribed to spin migration, or to unpaired spin delocalization over a large number of chlorophyll molecules. The linewidth of Signal I can be accounted for by a similar delocalization process. A theoretical relationship between the esr linewidth and the number of chlorophyll molecules, N, over which an unpaired spin is delocalized, takes the form ΔHN = 1/√N·ΔHM, where ΔHM is the linewidth of monomer (Chl·L)+.. This relationship for N = 2 accounts well for the linewidths of Signal I in green algae, blue-green algae, and photosynthetic bacteria in both the 1H- and 2H-forms. The linewidth of Signal I (as well as the optical properties of reaction-center chlorophyll) are consistent with unpaired spin delocalization over an entity containing two chlorophyll molecules, (Chl·H2O·Chl)+..

https://www.pnas.org/content/pnas/68/3/625.full.pdf

Electron Spin Resonance of Chlorophyll and the Origin of Signal I in Photosynthesis

Studies with Deuterated Drugs

An analysis of the visible absorption spectrum of chlorophyll a monomer, dimer,and oligomers in solution.

Nuclear Magnetic Resonance Spectra and Molecular Association of Chlorophylls a and b, Methyl Chlorophyllides, Pheophytins, and Methyl Pheophorbides

Preparation and properties of pyrochlorophyll a, methyl pyrochlorophyllide a, pyropheophytin a, and methyl pyropheophorbide a derived from chlorophyll by decarbomethoxylation

Joseph J. Katz

Papers

Electron Spin Resonance of Chlorophyll and the Origin of Signal I in Photosynthesis

Studies with Deuterated Drugs

An analysis of the visible absorption spectrum of chlorophyll a monomer, dimer,and oligomers in solution.

Nuclear Magnetic Resonance Spectra and Molecular Association of Chlorophylls a and b, Methyl Chlorophyllides, Pheophytins, and Methyl Pheophorbides

Preparation and properties of pyrochlorophyll a, methyl pyrochlorophyllide a, pyropheophytin a, and methyl pyropheophorbide a derived from chlorophyll by decarbomethoxylation