page_title: NADH peroxidase
section_title: Structure
hierarchical_section_title: NADH peroxidase / Structure
caption_attribution_description: English: Four residues essential for active site functionality in NADH Peroxidase. Adapted from RCSB Protein Bank PDB 2NPX.
context_page_description: In enzymology, a NADH peroxidase is an enzyme that catalyzes the chemical reaction
  NADH + H⁺ + H₂O₂ NAD⁺ + 2 H₂O
  The presumed function of NADH peroxidase is to inactivate H₂O₂ generated within the cell, for example by glycerol-3-phosphate oxidase during glycerol metabolism or dismutation of superoxide, before the H₂O₂ causes damage to essential cellular components.
  The 3 substrates of this enzyme are NADH, H⁺, and H₂O₂, whereas its two products are NAD⁺ and H₂O. It employs one cofactor, FAD, however no discrete FADH₂ intermediate has been observed.
  This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor. The systematic name of this enzyme class is NADH:hydrogen-peroxide oxidoreductase. Other names in common use include DPNH peroxidase, NAD peroxidase, diphosphopyridine nucleotide peroxidase, NADH-peroxidase, nicotinamide adenine dinucleotide peroxidase, and NADH2 peroxidase.
context_section_description: The crystal structure of NADH peroxidase resembles glutathione reductase with respect to chain fold and location as well as conformation of the prosthetic group FAD
  His10 of the NADH peroxidase is located near the N-terminus of the R1 helix within the FAD-binding site.  One of the oxygen atoms of Cys42-SO₃H is hydrogen-bonded both to the His10 imidazole and to Cys42 N terminus. The His10 functions in part to stabilize the unusual Cys42-SOH redox center. Arg303 also stabilizes the Cys42-SO₃H. Glu-14 participates in forming the tight dimer interface that limits solvent accessibility, important for maintaining the oxidation state of the sulfenic acid.
caption: Four residues essential for active site functionality in NADH Peroxidase, Adapted from PDB 2NPX
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