Metalloenzymes use metal ions in their active site to catalyze chemical transformation in a highly efficient manner. In order to achieve this unique capability, metalloproteins have evolved to maintain strict control over both the primary and secondary coordination spheres surrounding metal ions within active sites. They allow for fine tuning of the reactivity of the metal site. Thus, it is important to understand how the protein environment influences the chemistry at metal catalytic site by a combination of crystallography and X-ray spectroscopy. We are targeting transition metal based metalloenzymes and related systems to study the effect of the microenvironments that enables complicated chemistry in a sequential manner. Using simultaneous data collection of crystallography and X-ray spectroscopy at XFELs we study the interplay of metal sites and protein environment at room temperature. Some of the systems we have studied are methane monooxygenases (MMO), isopenicillin N synthase (IPNS), and ribonucleotide reductase (RNR), and other metalloenzymes related to energy are also being studied.