1Introduction Molybdenum (Mo) containing enzymes have been associated with the catalysis of important reactions in the metabolism of smallm oleculess uch as carbon nitrogen, and sulfur [1a, b].T he sulfite oxidizing enzymes sulfite oxidase (SO) and sulfite dehydrogenase (SDH) catalyze the oxidation of sulfite to sulfate accompaniedw ith the release of two electrons and two protons according to the following equation:All sulfite oxidizing enzymes share the same catalytic Mo cofactor (Moco) containingu nit. But the number and type of additional redoxc enters differb etween enzymes from different classes of organisms, which has an impact on the type of electrona cceptor the enzyme can use [2a, b].O nly in the vertebrate SO ah eme b binding domaini sc ovalently linkedt ot he core structure of the enzyme.T he human sulfite oxidase (hSO) shows al arge structural homology to the enzyme from chicken liver (cSO) which is ad imeric enzyme where each subunit of the homodimer consists of an N-terminal heme b binding domain( SO-HD), followed by ap olypeptide tetherc onnectingt he heme domain to the Moco-containing domain (SO-MD) and ad imerization domain at the C-terminus [3].Thes ingle steps of the SO catalyzed reaction involve the two-electron oxidationo fs ulfite to sulfate at the Moco center, where Mo VI is reduced to Mo IV .I nv ertebrate SO the Mo VI regeneration is naturally coupled to the reduction of two equivalents of soluble cytochrome c which proceeds in two subsequent intra-and intermolecular singlee lectron transfer steps via the heme b5 containing site [4a, b, c].T hese steps involve ar epositioning of the domains to reduce electron transfer distances permitting electron transfer from Mo to Fe of SO-HD and to cytochrome c [5a, b].Areaction with soluble [6a, b] and polymerb ound redoxm ediators is also possible [7a, b]. Direct unmediated electron transfer from the reduced enzyme to electrodes proceedsv ia the hemed omain [8]. This process was most effective when the enzymei si mmobilized on electrode surfaces modified with positive charged SAMs facilitating the oriented assembly of SO electron transfer and bioelectrocatalysis [9a, b].Abstract:W er eport efficient bioelectrocatalytic sulfite oxidation by human sulfite oxidase (hSO) immobilizedo n ag old nanoparticle (AuNP)m odified gold electrode.T he AuNP were synthesized in aqueous phase by using branched polyethyleneimine (PEI) as reducing as well as stabilizing agent. Golde lectrodes were modified by as elf assembled monolayer of dithio-bis(N-hydroxysuccinimidyl propionate) (DTSP) onto which the NP and hSO were immobilized. Cyclic voltammetry of the hSO modified electrode in the absence of substrater evealedaquasi-reversible direct electrochemical reactiono ft he heme domaino fhSO with fast electron transfer rate.T he electron transferr ate constant of k s = 32 s À1 and the formal potential E 0 ' = À0.155 Vv s. Ag/AgCl/1 MK Cl were estimated. Comparatives tudies with nanoparticles of BaSO 4 indicate the importance of the NP conductivity for charge transfer an...