T. J. Erb

The paper shows that multiple mechanisms of essentiality in protein-protein interactions can persist over time, even if individual mechanisms are lost, using Rubisco as a case study.

The paper reports the cryogenic electron microscopy structure of the Fe nitrogenase complex from Rhodobacter capsulatus, revealing its active site architecture and subunit interactions.

This study engineers the ketosynthase domain of a polyketide synthase to enhance activity and shift specificity towards non-native extender units in vitro.

This paper investigates the structural and dynamic mechanisms of CO2 fixation by ECRs, revealing inter-subunit coupling that enables fast catalytic activity.

This study shows that adaptive evolution in E. coli can change cofactor specificity of enzymes, enabling NADPH regeneration without external sources, but is limited by thermodynamic constraints.

This study uses in vivo selection to engineer formate dehydrogenases with high efficiency and specificity for NADP+ regeneration.

The paper investigates how 4HBD, a key enzyme in archaeal carbon fixation, adapted structurally to become oxygen-tolerant, revealing evolutionary changes that enabled aerobic metabolism.