Cytochrome P450 monooxygenases (P450s) are versatile biocatalysts that perform a range of oxidative reactions with remarkable chemo-, regio-, and stereoselectivity. Their ability to functionalize unactivated C–H bonds makes them valuable for green and selective synthesis. However, most known P450s are derived from mesophilic microorganisms and show limited stability under industrial conditions. Using DNA metagenomics, we explored the microbial community of an Australian hot spring in northern Queensland to identify P450s adapted to extreme environments. Computational bioprospecting of the assembled metagenomes led to the identification of >200 putative thermostable P450s. Several were associated with thermophilic bacterial lineages, while others were unexpectedly linked to mesophilic taxa. Four representative enzymes from diverse P450 families were expressed and characterized. All are indeed thermostable, with melting temperatures of 48 – 65 °C, compared with <40 °C for mesophilic homologs. One of the challenges of employing thermostable P450s biotechnologically is obtaining suitable thermostable redox partners. Interestingly, none of the P450s expressed were associated with functional redox partners. However, one of these P450s is a CYP116, a family that has both redox partners and hemoprotein as domains on a single polypeptide. The characterisation and properties of these P450s will be discussed. Additionally, the X-ray crystal structure of a thermophilic CYP108 was solved, providing key structural insights to substrate binding and redox properties. Building upon the previous works, we introduced structure-based mutagenesis to enable peroxygenase activity in selected P450s. This study expands the repertoire of stable oxidative biocatalysts for sustainable synthesis of fine chemicals, pharmaceuticals, and natural products.