C07K14/80

Mutant Cytochrome Protein and Use Thereof

A mutant cytochrome protein originated from a cytochrome protein having three heme-binding domains, which mutant cytochrome protein lacks the first heme-binding domain and the second heme-binding domain as counted from the N-terminus, is provided. The mutant cytochrome protein may lack a region(s) containing the first and second heme-binding domains.

Mutant Cytochrome Protein and Use Thereof

A mutant cytochrome protein originated from a cytochrome protein having three heme-binding domains, which mutant cytochrome protein lacks the first heme-binding domain and the second heme-binding domain as counted from the N-terminus, is provided. The mutant cytochrome protein may lack a region(s) containing the first and second heme-binding domains.

COMPOSITIONS FOR THE PREVENTION AND TREATMENT OF PARKINSON'S DISEASE
20210122780 · 2021-04-29 ·

Methods of preventing or retarding or reversing or abolishing the onset of Parkinson's and other neurodegenerative diseases are discussed.

Mutant cytochrome protein and use thereof

A mutant cytochrome protein originated from a cytochrome protein having three heme-binding domains, which mutant cytochrome protein lacks the first heme-binding domain and the second heme-binding domain as counted from the N-terminus, is provided. The mutant cytochrome protein may lack a region(s) containing the first and second heme-binding domains.

Mutant cytochrome protein and use thereof

A mutant cytochrome protein originated from a cytochrome protein having three heme-binding domains, which mutant cytochrome protein lacks the first heme-binding domain and the second heme-binding domain as counted from the N-terminus, is provided. The mutant cytochrome protein may lack a region(s) containing the first and second heme-binding domains.

SYSTEMS AND METHODS FOR FORMING BIOLOGICAL NANOWIRES AND APPLICATIONS THEREOF
20210002332 · 2021-01-07 · ·

A nanowire may be isolated from a bacterium, wherein the nanowire includes c-type heme subunits or pili proteins and is capable of establishing an electrical connection with an insoluble electron acceptor. The c-type heme subunits may comprise OmcS or OmcZ cytochrome subunits or any combination thereof. The pili proteins may have an amino acid sequence with at least one residue modified, from a wild-type strain of the microorganism, to include an aromatic amino acid. The nanowire may have metallic or semiconducting conductive properties, and may be integrated into an electronic device.

SYSTEMS AND METHODS FOR FORMING BIOLOGICAL NANOWIRES AND APPLICATIONS THEREOF
20210002332 · 2021-01-07 · ·

A nanowire may be isolated from a bacterium, wherein the nanowire includes c-type heme subunits or pili proteins and is capable of establishing an electrical connection with an insoluble electron acceptor. The c-type heme subunits may comprise OmcS or OmcZ cytochrome subunits or any combination thereof. The pili proteins may have an amino acid sequence with at least one residue modified, from a wild-type strain of the microorganism, to include an aromatic amino acid. The nanowire may have metallic or semiconducting conductive properties, and may be integrated into an electronic device.

FUSION PROTEIN OF FLAVIN ADENINE DINUCLEOTIDE-GLUCOSE DEHYDROGENASE AND CYTOCHROME MOLECULE

The purpose of the present invention is to provide a fungus-derived FADGDH that has a direct electron transfer ability. Provided is a fusion protein comprising a fungus-derived FADGDH or a mutant thereof and a cytochrome molecule connected to the N-terminus of the FADGDH or variant thereof.

FUSION PROTEIN OF FLAVIN ADENINE DINUCLEOTIDE-GLUCOSE DEHYDROGENASE AND CYTOCHROME MOLECULE

The purpose of the present invention is to provide a fungus-derived FADGDH that has a direct electron transfer ability. Provided is a fusion protein comprising a fungus-derived FADGDH or a mutant thereof and a cytochrome molecule connected to the N-terminus of the FADGDH or variant thereof.

NOVEL P450-BM3 VARIANTS WITH IMPROVED ACTIVITY

The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates.