John Rubinstein
@johnrubinstein.bsky.social
CryoEM, Bioenergetics, V-ATPases (especially in synaptic vesicles and lysosomes), OxPhos (especially in mycobacteria as a TB drug target)
Scientist, The Hospital for Sick Children
Professor, U of Toronto
👨👩👧🔬🚲
rubinsteinlab.org
COI: structura.bio
Scientist, The Hospital for Sick Children
Professor, U of Toronto
👨👩👧🔬🚲
rubinsteinlab.org
COI: structura.bio
Adding short-chain acyl-CoA substrate (plus ATP & bicarbonate) causes biotin carboxyl carrier protein (BCCP) domains to travel between biotin carboxylase (BC) domains, which load a carboxyl group onto the BCCP biotin, and the carboxyltransferase (CT) domain, which transfers it to the acyl-CoA.
October 30, 2025 at 3:21 AM
Adding short-chain acyl-CoA substrate (plus ATP & bicarbonate) causes biotin carboxyl carrier protein (BCCP) domains to travel between biotin carboxylase (BC) domains, which load a carboxyl group onto the BCCP biotin, and the carboxyltransferase (CT) domain, which transfers it to the acyl-CoA.
One of the iron-sulfur clusters (D1) is a linear [3Fe-4S] cluster that has been synthesized chemically and detected spectroscopically but has not been seen before in the structure of a protein under physiological conditions
May 16, 2025 at 2:30 PM
One of the iron-sulfur clusters (D1) is a linear [3Fe-4S] cluster that has been synthesized chemically and detected spectroscopically but has not been seen before in the structure of a protein under physiological conditions