Enzymatic activity mastered by altering metal coordination spheres.
Metalloenzymes control enzymatic activity by changing the characteristics of the metal centers where catalysis takes place. The conversion between inactive and active states can be tuned by altering the coordination number of the metal site, and in some cases by an associated conformational change. These processes will be illustrated using heme proteins (cytochrome c nitrite reductase, cytochrome c peroxidase and cytochrome cd1 nitrite reductase), non-heme proteins (superoxide reductase and [NiFe]-hydrogenase), and copper proteins (nitrite and nitrous oxide reductases) as examples. These examples catalyze electron transfer reactions that include atom transfer, abstraction and insertion.
Moura
Isabel
I
REQUIMTE, Centro de Química Fina e Biotecnologia, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal. isa@dq.fct.unl.pt
Pauleta
Sofia R
SR
Moura
José J G
JJ
D020134:Catalytic Domain; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D006420:Hemeproteins / Q000737:chemistry / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism*; D008670:Metals / Q000737:chemistry* / Q000378:metabolism*
D004798:Enzymes; D006420:Hemeproteins; D008667:Metalloproteins; D008670:Metals; D006418:Heme