The Structure of the Small Laccase from Streptomyces coelicolor Reveals a Link between Laccases and Nitrite Reductases

Skálová, Tereza; Dohnálek, Jan; Østergaard, Lars; Østergaard, Per; Kolenko, Petr; Dušková, Jarmila; Štěpánková, Andrea; Hašek, Jindřich

doi:10.1016/j.jmb.2008.11.024

Cited by 138 publications

(166 citation statements)

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“…It is worth noting that this LAC is structurally different to the others, being organized as a trimer. [187] SAM-functionalized gold electrodes and gold nanoparticles (NPs) with anthracenethiol derivatives, [188] or phenyl groups ending either with amino or carboxyl functions were also evaluated as platforms for efficient orientation of Trametes versicolor (Tv), Tt and Trametes hirsute (Th) LACs. [189][190][191] PMIRRAS, QCM, and electrochemistry were coupled and allowed a specific orientation linked to a different activity of the enzyme depending on the functionality borne by the SAM to be demonstrated.…”

Section: Multicopper Oxidases (Mcos)mentioning

confidence: 99%

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

et al. 2014

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Among sustainable alternatives to fossil fuel, proton exchange membrane fuel cells are promising devices that deliver electricity from hydrogen and oxygen, producing only water. The transformation of the fuel and oxidant however relies on rare‐metal catalysts. H2/O2 enzymatic biofuel cells thus emerge as sustainable biotechnological devices in which chemical catalysts are replaced by hydrogenases at the anode and multicopper oxidases at the cathode. This review discusses the recent breakthroughs and the limitations in all the components of H2/O2 biofuel cells: 1) Catalytic mechanisms involved in multicopper oxidases and hydrogenases, in addition to the new potential of enzymes from the biodiversity pool, which exhibit outstanding properties. 2) The molecular basis for oriented enzyme immobilization on the electrochemical interfaces as a prerequisite for a fast direct electron‐transfer rate. 3) The requirement for 3D networks to enhance current densities. 4) The production of H2 from biomass. 5) The history of H2/O2 biofuel cells and recent devices, which also highlights the remaining issues that will allow the use of such devices in low‐power applications.

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Section: Multicopper Oxidases (Mcos)mentioning

confidence: 99%

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

et al. 2014

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“…Likewise, the recombinant laccase of Trametes villosa in A. oryzae was investigated to elucidate the reaction mechanism of the reduction of dioxygen to water by stopped-flow experiments and under steady-state conditions. 134 Moreover, the availability of high yields of recombinant proteins has allowed solving 3D structures of the laccase from Coprinus cinereus 139 and bacterial laccase from S. coelicolor expressed in A. oryzae, 144 and that from M. albomyces expressed in T. reesei.…”

Section: Recombinant Laccases As Tools For Greening Industrymentioning

confidence: 99%

Heterologous laccase production and its role in industrial applications

Piscitelli¹,

Pezzella²,

Giardina³

et al. 2010

Bioengineered Bugs

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“…The physiological role of the 2dMCOs is not clear, but the biochemical data indicate substrate specificities similar to three-domain laccases (15)(16)(17)(18). The crystal structure of the type B 2dMCO SLAC was recently determined to 2.7 Å resolution and revealed a homotrimer with an overall architecture similar to NIRs (19). To further understand 2dMCOs and the relationships between NIRs and MCOs, we have determined the crystal structure of a type C 2dMCO, BCO from N. europaea, to 1.9 Å resolution.…”

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Crystal Structure of a Two-domain Multicopper Oxidase

Lawton

Sayavedra-Soto

Arp

et al. 2009

Journal of Biological Chemistry

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The two-domain multicopper oxidases are proposed to be key intermediates in the evolution of three-domain multicopper oxidases. A number of two-domain multicopper oxidases have been identified from genome sequences and are classified as type A, type B, or type C on the basis of the predicted location of the type 1 copper center. The crystal structure of blue copper oxidase, a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been determined to 1.9 Å resolution. Blue copper oxidase is a trimer, of which each subunit comprises two cupredoxin domains. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The coordination geometry at the trinuclear copper site is consistent with reduction of the copper ions. Although the overall architecture of blue copper oxidase is similar to nitrite reductases, detailed structural alignments show that the fold and domain orientation more closely resemble the three-domain multicopper oxidases. These observations have important implications for the evolution of nitrite reductases and multicopper oxidases. Multicopper oxidases (MCOs)2 are a widely distributed class of enzymes with diverse functions ranging from copper and iron metabolism to polyphenol oxidation. MCOs contain four copper ions arranged in two sites: a blue type 1 mononuclear copper center (T1) and a trinuclear copper cluster (T2/T3) consisting of a normal type 2 copper center (T2) and dinuclear type 3 (T3) center (1-3). Substrate oxidation is coupled to reduction of dioxygen to water via electron transfer from the T1 site to the T2/T3 cluster where dioxygen binds (4, 5). Because of structural similarities, MCOs are often grouped with copper nitrite reductases (NIRs), which contain both T1 and T2 sites (6), and are collectively referred to as multicopper blue proteins (MCBPs) (7). MCOs are composed of multiple cupredoxin domains, and both three-domain and six-domain variants have been studied. Three-domain MCOs (3dMCOs) include ascorbate oxidase, laccases, CueO, and Fet3. In these proteins, the T1 site is located in the C-terminal cupredoxin domain, and the T2/T3 cluster is located at the interface between domains 1 and 3 (8, 9). Ceruloplasmin is a six-domain MCO that houses T1 sites in domains 2, 4, and 6 and a T2/T3 cluster between domains 1 and 6 (10).Because of the prevalence of cupredoxin domains, blue copper proteins, and MCOs in nature, understanding their origins has the potential for addressing important questions about the evolution of protein size, function, structure, and complexity (11). Several models for the evolution of three-and six-domain MCOs have been proposed. In these models, the key evolutionary intermediates are two-domain ancestral MCOs (7,11,12). The two-domain MCOs (2dMCOs) are hypothesized to result from a single domain duplication event and have architectures resembling the homotrimeric two-domain NIRs. NIRs contain a T1 site in each domain 1 and a T2 site at the intersubunit interfaces betwee...

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The Structure of the Small Laccase from Streptomyces coelicolor Reveals a Link between Laccases and Nitrite Reductases

Cited by 138 publications

References 39 publications

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

Heterologous laccase production and its role in industrial applications

Crystal Structure of a Two-domain Multicopper Oxidase

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The Structure of the Small Laccase from Streptomyces coelicolor Reveals a Link between Laccases and Nitrite Reductases

Cited by 138 publications

References 39 publications

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

Heterologous laccase production and its role in industrial applications

Crystal Structure of a Two-domain Multicopper Oxidase

Contact Info

Product

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Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective