Contact Information
600 S Mathews
M/C 712
Urbana, IL 61801
Research Areas
Research Description
The Crofts Lab explored structure/function relationships in photosynthetic energy conversion; structure of membrane proteins; mechanism of energy conservation; photosynthesis in intact plants; and the flux of energy through the biosphere. These contributions have been recognized through the Honors and Awards listed below. Professor Crofts' recent interests have extended to the flux of information through the biosphere, and from there to the Entanglement problem. Examination of the latter calls in to question the current consensus (as recognized by three Nobel laureates in 2022) that Bell's Inequalities show a world at the quantum level that is non-local, and suggests that Einstein's local realism provides a better, more economical, model. Three papers on this topic (see below) and near completion, and are available from the author on request by e-mail to crofts@illinois.edu.
(Crofts, A. R. (2025) Entanglement re-examined: 1 simulation of Einstein’s model shows that Bell’s inequalities do not exclude local realism
(Crofts, A. R. (2025) Entanglement re-examined: 2. Maybe Einstein got it right
(Crofts, A. R. (2025) Photons, Gravitons, and a “Theory of Everything”
Honors
1957 State Scholarship.
1958-61 Major Scholar in Natural Science, Gonville and Caius College, U. of Cambridge.
1961 Medical Research Council Research Studentship.
1974 Reader in Biochemistry, University of Bristol.
1982 Melandri Lecture and Medal, 2nd. EBEC Meeting, Lyon.
1983 Francis I Medal, College de France
1985 John Simon Guggenheim Fellow.
1989-92 University Senior Scholar, University of Illinois at Urbana-Champaign
1991 Fellow, American Association for the Advancement of Science
1992 C.F. Kettering Award and Prize, American Society for Plant Physiology.
2004 Lars Ernster Memorial Lecture, Stockholm
2022 Peter Mitchell Medal awarded at the European Bioenergetics Conference (EBEC), 2022
Education
B.A. 1961 University of Cambridge, U.K.
Ph.D. 1965 University of Cambridge, U.K.
Postdoc. 1965-66, Dept. of Physiology, U.C., Berkeley
Additional Campus Affiliations
Beckman Institute
External Links
Highlighted Publications
Representative Publications
1. Crofts, A. R. (2021) The modified Q-cycle: A look back at its development and forward to a functional model. Biochim. Biophys. Acta, - Bioenergetics 1862, 148417-148459
2. Crofts, A.R. (2007) Life, information, entropy, and time. Complexity, 13, 14-50 (PMC2577055)
3. Crofts, A.R., Holland, J.T., Victoria, D., Kolling D.R.J., Dikanov, S.A., Gilbreth, R., Lhee, S., Kuras, R., and Guergova-Kuras, M. (2008) The Q-cycle reviewed: How well does a monomeric mechanism of the bc1 complex account for the function of a dimeric complex? Biochim. Biophys. Acta, 1777, 1001-1019 (PMC2578832)
4. Kolling, D.R.J., Samoilova, R.I., Shubin, A.A., Crofts, A.R. and Dikanov, S. A. (2009) Proton Environment of Reduced Rieske Iron-Sulfur Cluster Probed by Two-Dimensional ESEEM Spectroscopy. J. Phys. Chem. 113, 653-667 (PMC2773023)
5. Dikanov, S.A., Samoilova, R.I., Kappl, R., Crofts, A.R. and Hüttermann, J. (2009) The reduced [2Fe-2S] clusters in adrenodoxin and ferredoxin share spin density with protein nitrogens, probed using 2D ESEEM. Phys. Chem. Chem. Phys. 11, 6807-6819 (PMC2773023)
6. Lhee, S., Kolling, D. R., Nair, S. K., Dikanov, S. A. and Crofts, A. R. (2010) Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: Effects on the biophysical properties of the Rieske iron-sulfur protein and on the kinetics of the complex. J. Biol. Chem. 285, 9233-9248 (PMC2838342)
7. S. Hong, D. Victoria, A.R. Crofts, Inter-monomer electron transfer is too slow to compete with monomeric turnover in bc1 complex. Biochim. Biophys. Acta, 1817 (2012) 1053-1062.
8. Victoria, D., Burton, R., Crofts, A.R. (2013) Role of the -PEWY-glutamate in catalysis at the Qo-site of the cyt bc1 complex. Biochim. Biophys. Acta 1827, 365-386.
9. Crofts, A. R., Hong, S., Wilson, C., Burton, R., Victoria, D., Harrison, C., Schulten, K. (2013) The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex. Biochim. Biophys. Acta 1827, 1362–1377