JUDITH POLLOCK KLINMAN
Affiliation: University of California
Klinman J. How do enzymes activate oxygen without inactivating themselves?. Acc Chem Res. 2007;40:325-33 pubmed
..These permit a controlled reactivity of oxygen to generate the desired regio- and stereochemical products, while minimizing deleterious side reactions. ..
Zhu W, Martins A, Klinman J. Methods for Expression, Purification, and Characterization of PqqE, a Radical SAM Enzyme in the PQQ Biosynthetic Pathway. Methods Enzymol. 2018;606:389-420 pubmed publisher
..Here, we summarize the methods developed in our lab for the expression and purification of PqqE. We also highlight the several methods we have used for the characterization of the enzyme. ..
Klinman J, Kohen A. Evolutionary aspects of enzyme dynamics. J Biol Chem. 2014;289:30205-12 pubmed publisher
Zhang J, Klinman J. High-performance liquid chromatography separation of the (S,S)- and (R,S)-forms of S-adenosyl-L-methionine. Anal Biochem. 2015;476:81-3 pubmed publisher
..Here, we have developed a chromatographic method to obtain pure (S,S)-AdoMet using a single C18 column. ..
Latham J, Iavarone A, Barr I, Juthani P, Klinman J. PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway. J Biol Chem. 2015;290:12908-18 pubmed publisher
..In conclusion, we propose that PqqD is a novel peptide chaperone and that PqqD orthologues may play a similar role in peptide modification pathways that use an RS-SPASM protein. ..
Zhang J, Kulik H, Martinez T, Klinman J. Mediation of donor-acceptor distance in an enzymatic methyl transfer reaction. Proc Natl Acad Sci U S A. 2015;112:7954-9 pubmed publisher
..These experimental and computational results are discussed in the context of active site compaction that requires an ionization of substrate within the enzyme ternary complex. ..
Barr I, Latham J, Iavarone A, Chantarojsiri T, Hwang J, Klinman J. Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD. J Biol Chem. 2016;291:8877-84 pubmed publisher
..These results indicate that PqqE, in conjunction with PqqD, carries out the first step in PQQ biosynthesis: a radical-mediated formation of a new carbon-carbon bond between two amino acid side chains on PqqA. ..
Collazo L, Klinman J. Control of the Position of Oxygen Delivery in Soybean Lipoxygenase-1 by Amino Acid Side Chains within a Gas Migration Channel. J Biol Chem. 2016;291:9052-9 pubmed publisher
..The present data indicate that modest changes in a protein scaffold may modulate the access of small gaseous molecules to enzyme-bound substrates. ..
Hu S, Cattin Ortolá J, Munos J, Klinman J. Hydrostatic Pressure Studies Distinguish Global from Local Protein Motions in C-H Activation by Soybean Lipoxygenase-1. Angew Chem Int Ed Engl. 2016;55:9361-4 pubmed publisher