@Article{IPB-486,
author = {Münch, J. and Püllmann, P. and Zhang, W. and Weissenborn, M. J.},
title = {{Enzymatic Hydroxylations of sp3-Carbons}},
year = {2021},
pages = {9168-9203},
journal = {ACS Catal.},
doi = {10.1021/acscatal.1c00759},
volume = {11},
abstract = {Enzymatic hydroxylation of activated and nonactivated sp3-carbons
 attracts keen interest from the chemistry community as it is one of the
 most challenging tasks in organic synthesis. Nature provides a vast 
number of enzymes with an enormous catalytic versatility to fulfill this
 task. Given that those very different enzymes have a distinct 
specificity in substrate scope, selectivity, activity, stability, and 
catalytic cycle, it is interesting to outline similarities and 
differences. In this Review, we intend to delineate which enzymes 
possess considerable advantages within specific issues. Heterologous 
production, crystal structure availability, enzyme engineering 
potential, and substrate promiscuity are essential factors for the 
applicability of these biocatalysts.}    
}