Molecular dynamics simulations of mouse ferrochelatase variants: what distorts and orientates the porphyrin?

• Tipo: Artigo em Revista Científica Internacional
• Data: 2009

Autores

Borys Szefczyk (Autor) Outra; Natalia N D S Cordeiro (Autor) FCUP; Ricardo Franco (Autor) Outra; Jose A N F Gomes (Autor) FCUP

Revista

Título: Journal of Biological Inorganic Chemistry

Vol. 14

Páginas: 1119-1128

ISSN: 0949-8257

Editora: Springer Nature

Indexação

ISI Web of Knowledge - 4 Citações

Scopus - 4 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Química

Outras Informações

ID Authenticus: P-003-G7A

DOI: 10.1007/s00775-009-0556-y

Abstract (EN): Molecular dynamics simulations of the wild-type and variant forms of the mouse ferrochelatase in complex with the product (haem) have been performed using the GROMOS96 force field, in the NpT ensemble. Ferrochelatase, the last enzyme in the catalytic pathway of the haem biosynthesis, catalyses the reaction of insertion of a ferrous ion into protoporphyrin IX by distorting the planar geometry of the latter reactant. The simulations presented aim at understanding the role of active-site residues in this catalytic process. Analysis of the simulation trajectories explains the consequences of the mutations introduced and sheds more light on the role of the His209 residue in porphyrin macrocycle distortion. The function of residues coordinating propionate groups of the haem molecule is discussed in terms of stability of the substrate and product complexes.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 10