title: Empirical and computational design of iron-sulfur cluster proteins.
abstract: Here, we compare two approaches of protein design. A computational approach was used in the design of the coiled-coil iron-sulfur protein, CCIS, as a four helix bundle binding an iron-sulfur cluster within its hydrophobic core. An empirical approach was used for designing the redox-chain maquette, RCM as a four-helix bundle assembling iron-sulfur clusters within loops and one heme in the middle of its hydrophobic core. We demonstrate that both ways of design yielded the desired proteins in terms of secondary structure and cofactors assembly. Both approaches, however, still have much to improve in predicting conformational changes in the presence of bound cofactors, controlling oligomerization tendency and stabilizing the bound iron-sulfur clusters in the reduced state. Lessons from both ways of design and future directions of development are discussed. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial.
authors.affiliation: Institute of Physics, PAS, Warsaw, Poland. jgrzyb@ifpan.edu.pl
authors.forename: Joanna
authors.initials: J
authors.lastname: Grzyb
authors.forename: Fei
authors.initials: F
authors.lastname: Xu
authors.forename: Vikas
authors.initials: V
authors.lastname: Nanda
authors.forename: Renata
authors.initials: R
authors.lastname: Luczkowska
authors.forename: Eduard
authors.initials: E
authors.lastname: Reijerse
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Lubitz
authors.forename: Dror
authors.initials: D
authors.lastname: Noy
mesh_terms: D000595:Amino Acid Sequence; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
chemical_list: D007506:Iron-Sulfur Proteins