Topic
Multicopper oxidase
About: Multicopper oxidase is a research topic. Over the lifetime, 416 publications have been published within this topic receiving 24063 citations.
Papers published on a yearly basis
Papers
TL;DR: Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers.
Abstract: Copper is an essential trace element in living systems, present in the parts per million concentration range. It is a key cofactor in a diverse array of biological oxidation-reduction reactions. These involve either outer-sphere electron transfer, as in the blue copper proteins and the Cu{sub A} site of cytochrome oxidase and nitrous oxide redutase, or inner-sphere electron transfer in the binding, activation, and reduction of dioxygen, superoxide, nitrite, and nitrous oxide. Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 (T1) or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers. 428 refs.
3,539 citations
TL;DR: Characterization of this disorder revealed a critical physiological role for ceruloplasmin in determining the rate of iron efflux from cells with mobilizable iron stores and has provided new insights into human iron metabolism and nutrition.
Abstract: Ceruloplasmin is a serum ferroxidase that contains greater than 95% of the copper found in plasma. This protein is a member of the multicopper oxidase family, an evolutionarily conserved group of proteins that utilize copper to couple substrate oxidation with the four-electron reduction of oxygen to water. Despite the need for copper in ceruloplasmin function, this protein plays no essential role in the transport or metabolism of this metal. Aceruloplasminemia is a neurodegenerative disease resulting from inherited loss-of-function mutations in the ceruloplasmin gene. Characterization of this disorder revealed a critical physiological role for ceruloplasmin in determining the rate of iron efflux from cells with mobilizable iron stores and has provided new insights into human iron metabolism and nutrition.
921 citations
TL;DR: This work presents the first crystal structure of an active laccase containing a full complement of coppers, the complete polypeptide chain together with seven carbohydrate moieties, and a mechanism is presented to explain how laccases could tune their redox potential by as much as 200 mV.
916 citations
TL;DR: Two proteins in the plasma membrane of yeast—a multicopper oxidase and a permease, encoded by the FTR1 gene—were shown to mediate high-affinity iron uptake and played a direct role in iron transport.
Abstract: Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast—a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene—were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.
697 citations
TL;DR: It is suggested that the catalytic activity of the Fet3 protein is required for cellular iron accumulation, similar to that of the blue multicopper oxidoreductases.
697 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 15 |
| 2024 | 18 |
| 2023 | 13 |
| 2022 | 25 |
| 2021 | 23 |
| 2020 | 15 |