Match List I with List II

List I (Metalloprotein)	List II (Metal)
A. carboxypeptidase A	I. Mn
B. oxygen-evolving complex	II. Fe
C. hemerythrin	III. Ni
D. coenzyme F-430	IV. Zn

Choose the correct answer from the options given below:

Correct option is B

Cofactor F₄₃₀

F₄₃₀ is the cofactor (sometimes called the coenzyme) of the enzyme methyl coenzyme M reductase (MCR). 

$$CH_3\text{-}S\text{-}CoM + HS\text{-}CoB \rightarrow CH_4 + CoB\text{-}S\text{-}S\text{-}CoM$$

Coenzyme F₄₃₀ features a reduced porphyrin in a macrocyclic ring system called a corphin. In addition, it possesses two additional rings in comparison to the standard tetrapyrrole (rings A-D), having a γ-lactam ring E and a keto-containing carbocyclic ring F. It is the only natural tetrapyrrole containing nickel, an element rarely found in biological systems.

Oxygen-evolving complex

The oxygen-evolving complex (OEC), also known as the water-splitting complex, is a water-oxidizing enzyme involved in the photo-oxidation of water during the light reactions of photosynthesis. OEC is surrounded by 4 core proteins of photosystem II at the membrane-lumen interface. The mechanism for splitting water involves absorption of three photons before the fourth provides sufficient energy for water oxidation. The complex can exist in 5 states, denoted S₀ to S₄, with S₀ the most reduced and S₄ the most oxidized. Energy from the photons captured by photosystem II moves the system from state S₀ to S₁ to S₂ to S₃ and finally to S₄. S₄ reacts with water producing free oxygen:

$$2 H_2O \rightarrow O_2 + 4 H^+ + 4 e^-$$

This conversion resets the catalyst to the S₀ state. The active site of the OEC consists of a cluster of manganese and calcium. The mechanism of the complex is proposed to involve an Mn-oxide which couples by O-O bond formation to a calcium oxide/hydroxide.

Carboxypeptidase-A

Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains. Carboxypeptidase A (CPA) contains a zinc (Zn²⁺) metal center in a tetrahedral geometry with amino acid residues in close proximity around zinc to facilitate catalysis and binding.

Hemerythrin

Hemerythrin is an oligomeric protein responsible for oxygen (O₂) transport in the marine invertebrate phyla of sipunculids, priapulids, brachiopods, and in a single annelid worm genus, Magelona. Myohemerythrin is a monomeric O₂-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state. The mechanism of dioxygen binding is unusual. Most O₂ carriers operate via formation of dioxygen complexes, but hemerythrin holds the O₂ as a hydroperoxide (HO₂, or -OOH^-). The site that binds O₂ consists of a pair of iron centres.