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John Golbeck

Professor of Biochemistry and Biophysics
Professor of Chemistry

310 South Frear Laboratory, University Park, PA 16802
Phone: (814) 865-1163
Fax: (814) 863-7024
E-mail: jhg5@psu.edu

B.S. in Chemistry from Valparaiso University
Ph.D. in Chemistry from Indiana University

Golbeck Lab Web Site

Research
Bioassembly of Photosystem I in Cyanobacteria and Plants

Figure 2.2. Side view of Photosystem I showing the PsaA and PsaB heterodimer (red and blue helices), the FX, FB and FA iron-sulfur clusters (golden cubes) and the stromal polypepetides PsaC (magenta), PsaD (green) and PsaE (yellow).

The detailed molecular mechanisms of the bioassembly of the photosynthetic reaction centers are not well understood. What is known with certainty is that the last steps in the process include the assembly of the FX cluster, the binding of the stromal polypeptide PsaC (which contains the FA and FB clusters) and the subsequent binding of the stromal polypeptides PsaD and PsaE (Figure 2.2). The PsaC subunit, in turn, binds to the PS I core only when the FX, FA and FB clusters are present. Hence, the assembly of the Fe/S clusters is the key to the final steps in the binding of the stromal subunits. My students and I are taking two approaches to the bioassembly of Photosystem I. One involves the use of magnetic resonance spectroscopy to study the assembly of the stromal polypeptides PsaC, PsaD and PsaE. The other involves the use of molecular biology to study the assembly of the electron transfer cofactors, particularly the iron-sulfur clusters FX, FB and FA.

If you would like to learn more about individual projects, please follow these links:
Assembly of the Stromal Polypeptides PsaC, PsaD and PsaE on the Photosystem I Core
Involvement of the suf Regulon in Assembly of Photosynthetic Fe/S Clusters
Involvement of rubA in the Assembly of the FX Iron-Sulfur Cluster
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