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A) "Your answer".
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Running Head: EXAMINING FE-S PROTEIN STRUCTURE
Examining Fe-S Protein Structure
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1
EXAMINING FE-S PROTEIN STRUCTURE
2
Examining Fe-S Protein Structure
Part 1
Examining Fe-S Protein Structure
(A.)
1. The secondary structure that predominates in the protein is cysteine (α helix). This
secondary structure is formed as a result of joining molecules to form a water solvent amino
acid. α helix forms residues whose structure is essential is maintaining the rigidity of the protein.
2 The secondary elements that were present in the beta-grasp domain is known as ferredoxin
which is written as Fe2S2. Its primary function in real-life photosynthesis is to transfer electrons
to reductase enzyme which in turn make processes like assimilation possible. On top of that, the
ability of ferredoxin to oxidize or reduce is important in regulation of CO2.
(B.)
This domain is usually referred to as beta-grasp because the two active site consists of two disulphide which are bridged with high spin tetrahedral Iron three ions. Each of the atoms is
coordinated with two non-labile Sulphur atoms of the group terminal cystine. It can be
represented diagrammatically as shown below:
(C.)
With respect to the beta sheets in the subunit, the [2Fe-2S] cluster is located as a scaffolding
in the protein. Its environment is in such a way that it forms a pocket integrated within the
structure. This hydrophobic structure does not expose it to solvents.
(D.)
EXAMINING FE-S PROTEIN STRUCTURE
3
There exists a distinctive variation of how the two iron atoms are engrained in ...