FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4285086324> ?p ?o ?g. }

• W4285086324 abstract "Cumene dioxygenase (CumDO) is an initial enzyme in the cumene degradation pathway of Pseudomonas fluorescens IP01 and is a Rieske non-heme iron oxygenase (RO) that comprises two electron transfer components (reductase [CumDO-R] and Rieske-type ferredoxin [CumDO-F]) and one catalytic component (α3β3-type oxygenase [CumDO-O]). Catalysis is triggered by electrons that are transferred from NAD(P)H to CumDO-O by CumDO-R and CumDO-F. To investigate the binding mode between CumDO-F and CumDO-O and to identify the key CumDO-O amino acid residues for binding, we simulated docking between the CumDO-O crystal structure and predicted model of CumDO-F and identified two potential binding sites: one is at the side-wise site and the other is at the top-wise site in mushroom-like CumDO-O. Then, we performed alanine mutagenesis of 16 surface amino acid residues at two potential binding sites. The results of reduction efficiency analyses using the purified components indicated that CumDO-F bound at the side-wise site of CumDO-O, and K117 of the α-subunit and R65 of the β-subunit were critical for the interaction. Moreover, these two positively charged residues are well conserved in α3β3-type oxygenase components of ROs whose electron donors are Rieske-type ferredoxins. Given that these residues were not conserved if the electron donors were different types of ferredoxins or reductases, the side-wise site of the mushroom-like structure is thought to be the common binding site between Rieske-type ferredoxin and α3β3-type oxygenase components in ROs. IMPORTANCE We clarified the critical amino acid residues of the oxygenase component (Oxy) of Rieske non-heme iron oxygenase (RO) for binding with Rieske-type ferredoxin (Fd). Our results showed that Rieske-type Fd-binding site is commonly located at the stem (side-wise site) of the mushroom-like α3β3 quaternary structure in many ROs. The resultant binding site was totally different from those reported at the top-wise site of the doughnut-like α3-type Oxy, although α3-type Oxys correspond to the cap (α3 subunit part) of the mushroom-like α3β3-type Oxys. Critical amino acid residues detected in this study were not conserved if the electron donors of Oxys were different types of Fds or reductases. Altogether, we can suggest that unique binding modes between Oxys and electron donors have evolved, depending on the nature of the electron donors, despite Oxy molecules having shared α3β3 quaternary structures." @default.
• W4285086324 created "2022-07-14" @default.
• W4285086324 creator A5013777064 @default.
• W4285086324 creator A5032701666 @default.
• W4285086324 creator A5043420509 @default.
• W4285086324 creator A5051084085 @default.
• W4285086324 creator A5052407958 @default.
• W4285086324 creator A5054865826 @default.
• W4285086324 creator A5073136764 @default.
• W4285086324 creator A5082634879 @default.
• W4285086324 date "2022-08-09" @default.
• W4285086324 modified "2023-09-30" @default.
• W4285086324 title "The α- and β-Subunit Boundary at the Stem of the Mushroom-Like α ₃ β ₃ -Type Oxygenase Component of Rieske Non-Heme Iron Oxygenases Is the Rieske-Type Ferredoxin-Binding Site" @default.
• W4285086324 cites W1675570769 @default.
• W4285086324 cites W1777975588 @default.
• W4285086324 cites W1884448044 @default.
• W4285086324 cites W1933944259 @default.
• W4285086324 cites W1968410649 @default.
• W4285086324 cites W1970477004 @default.
• W4285086324 cites W1971336871 @default.
• W4285086324 cites W1975246115 @default.
• W4285086324 cites W1975264032 @default.
• W4285086324 cites W1976419711 @default.
• W4285086324 cites W1979813346 @default.
• W4285086324 cites W1980152562 @default.
• W4285086324 cites W1989383421 @default.
• W4285086324 cites W1994682835 @default.
• W4285086324 cites W2005897970 @default.
• W4285086324 cites W2010464084 @default.
• W4285086324 cites W2015547178 @default.
• W4285086324 cites W2016333765 @default.
• W4285086324 cites W2017583902 @default.
• W4285086324 cites W2020856504 @default.
• W4285086324 cites W2026982131 @default.
• W4285086324 cites W2035723736 @default.
• W4285086324 cites W2035916723 @default.
• W4285086324 cites W2048687101 @default.
• W4285086324 cites W2055611989 @default.
• W4285086324 cites W2062577852 @default.
• W4285086324 cites W2069301890 @default.
• W4285086324 cites W2074532774 @default.
• W4285086324 cites W2080324161 @default.
• W4285086324 cites W2084923757 @default.
• W4285086324 cites W2094123166 @default.
• W4285086324 cites W2095866056 @default.
• W4285086324 cites W2097382368 @default.
• W4285086324 cites W2100190822 @default.
• W4285086324 cites W2109515998 @default.
• W4285086324 cites W2118970998 @default.
• W4285086324 cites W2123177377 @default.
• W4285086324 cites W2123477091 @default.
• W4285086324 cites W2124272531 @default.
• W4285086324 cites W2129434797 @default.
• W4285086324 cites W2129669949 @default.
• W4285086324 cites W2130911289 @default.
• W4285086324 cites W2132629607 @default.
• W4285086324 cites W2132879814 @default.
• W4285086324 cites W2133891901 @default.
• W4285086324 cites W2145151004 @default.
• W4285086324 cites W2153255725 @default.
• W4285086324 cites W2158107035 @default.
• W4285086324 cites W2159614853 @default.
• W4285086324 cites W2163523836 @default.
• W4285086324 cites W2167738660 @default.
• W4285086324 cites W2171419407 @default.
• W4285086324 cites W2610096721 @default.
• W4285086324 cites W2751260413 @default.
• W4285086324 cites W2804822363 @default.
• W4285086324 cites W4234714728 @default.
• W4285086324 doi "https://doi.org/10.1128/aem.00835-22" @default.
• W4285086324 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35862661" @default.
• W4285086324 hasPublicationYear "2022" @default.
• W4285086324 type Work @default.
• W4285086324 citedByCount "3" @default.
• W4285086324 countsByYear W42850863242023 @default.
• W4285086324 crossrefType "journal-article" @default.
• W4285086324 hasAuthorship W4285086324A5013777064 @default.
• W4285086324 hasAuthorship W4285086324A5032701666 @default.
• W4285086324 hasAuthorship W4285086324A5043420509 @default.
• W4285086324 hasAuthorship W4285086324A5051084085 @default.
• W4285086324 hasAuthorship W4285086324A5052407958 @default.
• W4285086324 hasAuthorship W4285086324A5054865826 @default.
• W4285086324 hasAuthorship W4285086324A5073136764 @default.
• W4285086324 hasAuthorship W4285086324A5082634879 @default.
• W4285086324 hasBestOaLocation W42850863241 @default.
• W4285086324 hasConcept C103408237 @default.
• W4285086324 hasConcept C104292427 @default.
• W4285086324 hasConcept C104317684 @default.
• W4285086324 hasConcept C107824862 @default.
• W4285086324 hasConcept C134621786 @default.
• W4285086324 hasConcept C143065580 @default.
• W4285086324 hasConcept C165474305 @default.
• W4285086324 hasConcept C181199279 @default.
• W4285086324 hasConcept C185592680 @default.
• W4285086324 hasConcept C2776217839 @default.
• W4285086324 hasConcept C2776834422 @default.
• W4285086324 hasConcept C2779268744 @default.
• W4285086324 hasConcept C2779856020 @default.
• W4285086324 hasConcept C515207424 @default.
• W4285086324 hasConcept C55493867 @default.

• next